Kim Henrick - Academia.edu (original) (raw)
Papers by Kim Henrick
Proteins: Structure, Function, and Bioinformatics, 2004
Data management has emerged as one of the central issues in the high‐throughput processes of taki... more Data management has emerged as one of the central issues in the high‐throughput processes of taking a protein target sequence through to a protein sample. To simplify this task, and following extensive consultation with the international structural genomics community, we describe here a model of the data related to protein production. The model is suitable for both large and small facilities for use in tracking samples, experiments, and results through the many procedures involved. The model is described in Unified Modeling Language (UML). In addition, we present relational database schemas derived from the UML. These relational schemas are already in use in a number of data management projects. Proteins 2005. © 2004 Wiley‐Liss, Inc.
Journal of Molecular Biology, 1990
The following experimental techniques were used to determine the structure: X-RAY DIFFRACTION The... more The following experimental techniques were used to determine the structure: X-RAY DIFFRACTION The reported resolution of this entry is 2.50 Å. Percentile scores (ranging between 0-100) for global validation metrics of the entry are shown in the following graphic. The table shows the number of entries on which the scores are based. Metric Whole archive (#Entries) Similar resolution (#Entries, resolution range(Å)) Clashscore 141614 5346 (2.50-2.50) Ramachandran outliers 138981 5231 (2.50-2.50) Sidechain outliers 138945 5233 (2.50-2.50) The table below summarises the geometric issues observed across the polymeric chains and their t to the electron density. The red, orange, yellow and green segments on the lower bar indicate the fraction of residues that contain outliers for >=3, 2, 1 and 0 types of geometric quality criteria respectively. A grey segment represents the fraction of residues that are not modelled. The numeric value for each fraction is indicated below the corresponding segment, with a dot representing fractions <=5% Note EDS was not executed.
Journal of Biomolecular NMR, 2010
We present a suite of software for the complete and easy deposition of NMR data to the PDB and BM... more We present a suite of software for the complete and easy deposition of NMR data to the PDB and BMRB. This suite uses the CCPN framework and introduces a freely downloadable, graphical desktop application called CcpNmr Entry Completion Interface (ECI) for the secure editing of experimental information and associated datasets through the lifetime of an NMR project. CCPN projects can be created within the CcpNmr Analysis software or by importing existing NMR data files using the CcpNmr FormatConverter. After further data entry and checking with the ECI, the project can then be rapidly deposited to the PDBe using AutoDep, or exported as a complete deposition NMR-STAR file. In full CCPN projects created with ECI, it is straightforward to select chemical shift lists, restraint data sets, structural ensembles and all relevant associated experimental collection details, which all are or will become mandatory when depositing to the PDB.
Glycobiology, 2000
of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 h... more of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 has been extended to include N-terminal domain amino acid residues 91-113 containing one of the nine proline-rich motifs present in full-length hamster galectin-3. The modeling predicts two configurations of the N-terminal tail: in one the tail turns toward the first (SI) and last (S12) β-strands of the CRD and lies at the apolar dimer interface observed for galectins-1 and-2. In the second folding arrangement the N-terminal tail lies across the carbohydrate-binding pocket of the CRD where it could participate in sugar-binding: in particular tyrosine 102 and adjacent residues may interact with the partly solvent exposed nonreducing N-acetylgalactosamine and fucose substituents of the A-blood group structure GalNAcα1,3 [Fucα1,2]Galβ1,4GlcNAc-R. Binding studies using surface plasmon resonance of a recombinant fragment ∆1-93 protein containing residues 94-245 of hamster galectin-3 and a collagenase-derived fragment ∆1-103 containing residues 104-245, as well as alanine mutagenesis of residues 101-105 in ∆1-93 protein, support the prediction that Tyr102 and adjacent residues make significant contributions to oligosaccharide binding.
Analytical Sciences, 1994
Acta Crystallographica Section A Foundations of Crystallography, 2006
MrBUMP is a new automated procedure for structure solution by Molecular Replacement. The aim of M... more MrBUMP is a new automated procedure for structure solution by Molecular Replacement. The aim of MrBUMP is to start from native structure factors and a target sequence, and deliver a positioned and partly refined model, suitable for further model rebuilding , model completion and/or refinement. In the highest level view, the process consists of three stages. In the first stage, the target sequence is used to search for related proteins in the Protein Data Bank. This gives a list of template chains, domains and multimers, which is passed to the search model preparation stage. Up to three search models are generated for each template, differing in the alignment used and the treatment of side chains. Finally, given a list of putative search models, a subset is passed to the MR stage which uses Phaser or Molrep. Initial restrained refinement of the positioned model is used to assess the putative solution. MrBUMP consists of a set of Python scripts which link together established programs. MrBUMP differs from other molecular replacement pipelines in two ways: Firstly, there is a greater emphasis on the discovery of potential search models. A list of search models is generated and many are tried in molecular replacement with the aim of finding the optimum model. Secondly, Mr Bump is intended for general use within the CCP4 software suite, and is designed to be portable and flexible. m03.o04
Acta Crystallographica Section A Foundations of Crystallography, 2005
As the throughput of X-ray diffraction laboratories increases and the groups of users diversify, ... more As the throughput of X-ray diffraction laboratories increases and the groups of users diversify, the need for an automatic report generation system becomes more apparent. Although the type of report varies depending on the user's objectives, the data in the report is always based on information gathered throughout the experiment. We present a relational database approach to report generation. For each step of the structure determination the relevant pieces of information are recorded, such as the type of operation, input and output data, software version, user name, date and time. Furthermore, by linking the input of an operation to the output of the preceding steps, each piece of information is put into context as and when it becomes available. From the emerging tree structure it is possible to create a report from the beginning of the experiment to any step in the experiment. Wrong paths that did not lead to the final result are preserved too. Reports come in different shapes and sizes: various formats (e.g. CIF, mmCIF, HTML, and proprietary formats), various purposes (e.g. publication, archiving, or visualization), and varying degrees of detail. In order to serve this wide spectrum of needs we have developed a template language that describes which data is extracted from the database and how it is formatted.
Acta Crystallographica Section A Foundations of Crystallography, 2002
Acta Crystallographica Section A Foundations of Crystallography, 1993
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, 1978
The complex forms centrosymmetric [(CH3)2T1]2(D-tryptophan)(L-tryptophan) dimers in which each TI... more The complex forms centrosymmetric [(CH3)2T1]2(D-tryptophan)(L-tryptophan) dimers in which each TI atom is bonded to one O atom and one N atom of an amino acid residue with the carboxyl group acting as a monodentate bridging group [TI-C = 2.11 (1), 2.12 (1); TI-O = 2.47 (I), 2.59 (1); TIN = 2.66 (1) AI. The coordination at the Tl atom is irregular and a vacant sixth coordination site is taken up by an essentially non-bonding contact (3.43 A) from the pyrrole N atom of a parallel dimer set. Adjacent dimers in the crystal are held together in polymeric chains by hydrogen bonding between the molecule of water of crystallization and the pyrrole N-H.
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, 1978
F(000) = 372. The complex, (CHa)2TI(L-PHE), in the crystal consists of two independent polymeric ... more F(000) = 372. The complex, (CHa)2TI(L-PHE), in the crystal consists of two independent polymeric chains of (CH3)2Tl(L-phenylalanine) units linked by the carboxyl groups [T1-C = 2-06 (2), 2.15 (2); TI-O = 2.65 (1), 2.63 (1); T1-N = 2-53 (1) and TI~-C = 2.17 (2), 2.09 (2); Tll-O = 2.66 (1), 2.54 (1); TP-N = 2.53 (1) A]. Each independent Tl atom is approximately octahedrally coordinated with the sixth coordination site in each case occupied by a bridging carboxyl O atom of an adjacent polymeric chain [T1-O = 3.13, 3.06 Al.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2012
The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. T... more The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. The structure of TRAP consists of a central eight-stranded β-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit.
Journal of the Chemical Society, Dalton Transactions, 1988
Sulphonic acids RSO3H (R = CH3, CF3, or C6H4CH3-p) react with the precursors [MH2(CO)(PPh3)3](M =... more Sulphonic acids RSO3H (R = CH3, CF3, or C6H4CH3-p) react with the precursors [MH2(CO)(PPh3)3](M = Ru or Os) and [Ru(CO)3(PPh3)2] or [OsH2(CO)2(PPh3)2] in refluxing benzene or toluene to afford the complexes [M(O3SR)2(H2O)(CO)(PPh3)2] and [M(O3SR)2(CO)2(PPh3)2] respectively. The precursors [RuH2(PPh3)4] and [OsH4(PPh3)3] react with sulphonic acids in refluxing benzene to give the η6-benzene complexes [MH(η6-C6H6)(PPh3)2][O3SR]. However a similar reaction in refluxing ethanol yielded [OsH3(PPh3)4][O3SCF3]. The complexes [Ru(O3SR)2(H2O)(CO)(PPh3)2] have been shown by variable-temperature 1H and 31P-{1H} n.m.r. spectroscopy to be fluxional in solution. The solid-state structure of one example, [Ru(O3SC6H4CH3-p)2(H2O)(CO)(PPh3)2] has been determined by X-ray diffraction methods. The crystals are monoclinic, space group P21/n, with a= 24.382(5), b= 18.075(4), c= 10.729(2)A, β= 99.03(2)°, and Z= 4. The octahedral ruthenium(II) complex contains monodentate sulphonate ligands (trans to PPh3 and CO) and an aqua ligand (trans to PPh3) with strong hydrogen-bonding interactions between the H atoms of the H2O and the non-co-ordinated oxygen atoms of the sulphonate ligands. The molecular structure is very similar to that previously reported for the alcohol dehydrogenation catalyst [Ru(O2CCF3)2(CH3OH)(CO)(PPh3)2].
Journal of the Chemical Society, Dalton Transactions, 1986
ABSTRACT
Journal of the Chemical Society, Chemical Communications, 1980
Journal of the Chemical Society, Dalton Transactions, 1990
Prolonged photolysis of [Mo2(η-C5H5)2(µ-H)(µ-PMe2)(CO)4] in the presence of allene gives the new ... more Prolonged photolysis of [Mo2(η-C5H5)2(µ-H)(µ-PMe2)(CO)4] in the presence of allene gives the new complexes [Mo2(η-C5H5)2{µ-η5-CH2C(CH2)C(Me)CH2}(µ-PMe2)(CO)2] and [Mo2(η-C5H5)2(µ-PMe2){η3-CH2C(CH2)C(Me)CH2}(CO)3] the structures of which in the solid state have been determined by single-crystal X-ray analyses. The former of these new complexes is also obtained in the reaction of the µ-vinyl complex [Mo2(η-C5H5)2{µ-σ:η2-C(Me)CH2}(µ-PMe2)(CO)3] with allene but not in the reaction of the isomeric η3-allyl complex [Mo2(η-C5H5)2(µ-PMe2)-(η3-C3H5)(CO)3] with allene. On the other hand the syn-methylallyl complex [Mo(η-C5H5)2(µ-PMe2)(η3-syn-MeCHCH2CH2)(CO)3] does react with allene to give a ca. 1:2 inseparable mixture of [Mo2(η-C5H5)2{µ-η5-CH2C(CH2)C(Me)CHMe}(µ-PMe2)(CO)2] and [Mo2(η-C5H6)2{µσ:η5-CH2C(CH2)C(Et)CH2}(µ-PMe2)(CO)2]. These complexes may be obtained separately from reactions of the appropriate µ-vinyl complexes with allene. The mechanism of formation of the new complexes is discussed in the light of the above experimental results.
Journal of the Chemical Society, Dalton Transactions, 1984
The chlorohydridorhodium(III) complex of (o-diphenylphosphinophenyl)amine, [RhH(NH2C6H4PPh2-o)2Cl... more The chlorohydridorhodium(III) complex of (o-diphenylphosphinophenyl)amine, [RhH(NH2C6H4PPh2-o)2Cl]Cl (1a), formed by oxidative addition of HCl to [Rh(NH2C6H4PPh2-o)2]BF4(2b), was found to react with air to give two products. These have been characterised by X-ray structure analysis as the cis-dichloro-complex [Rh(NH2C6H4PPh2-o)(NHC6H4PPh2-o)Cl2](6), containing an amino- and amido-donor group, and the trans-dichloro-complex [Rh(NH2C6H4PPh2-o)2Cl2][p-MeC6H4SO3](8). Crystals of (6) are monoclinic, space group P21/n, with a= 17.153(3), b= 18.667(3), c= 9.891(2)A, β= 91.77(3)°, and Z= 4. Blocked full-matrix refinement using 3 501 unique data [I 3σ(I), 3 ⩽θ⩽ 25°] gave R= 0.0487, R′= 0.0511. Complex (8) crystallises, with a molecule of acetonitrile as solvate, in the monoclinic space group I2/c with a= 18.394(4), b= 14.380(3), c= 16.378(3)A, β= 96.67(4)°, and Z= 4. Blocked full-matrix refinement of 2 741 reflections with I 3σ(I)(3 ⩽θ⩽ 25°) gave R= 0.0638 and R′= 0.0698. The cation of (8) has exact C2 symmetry. A mechanism for the reaction is proposed which involves peroxo- and hydrogenperoxo-species.
Journal of the Chemical Society, Chemical Communications, 1982
ABSTRACT
Journal of the Chemical Society, Chemical Communications, 1980
ABSTRACT
Proteins: Structure, Function, and Bioinformatics, 2004
Data management has emerged as one of the central issues in the high‐throughput processes of taki... more Data management has emerged as one of the central issues in the high‐throughput processes of taking a protein target sequence through to a protein sample. To simplify this task, and following extensive consultation with the international structural genomics community, we describe here a model of the data related to protein production. The model is suitable for both large and small facilities for use in tracking samples, experiments, and results through the many procedures involved. The model is described in Unified Modeling Language (UML). In addition, we present relational database schemas derived from the UML. These relational schemas are already in use in a number of data management projects. Proteins 2005. © 2004 Wiley‐Liss, Inc.
Journal of Molecular Biology, 1990
The following experimental techniques were used to determine the structure: X-RAY DIFFRACTION The... more The following experimental techniques were used to determine the structure: X-RAY DIFFRACTION The reported resolution of this entry is 2.50 Å. Percentile scores (ranging between 0-100) for global validation metrics of the entry are shown in the following graphic. The table shows the number of entries on which the scores are based. Metric Whole archive (#Entries) Similar resolution (#Entries, resolution range(Å)) Clashscore 141614 5346 (2.50-2.50) Ramachandran outliers 138981 5231 (2.50-2.50) Sidechain outliers 138945 5233 (2.50-2.50) The table below summarises the geometric issues observed across the polymeric chains and their t to the electron density. The red, orange, yellow and green segments on the lower bar indicate the fraction of residues that contain outliers for >=3, 2, 1 and 0 types of geometric quality criteria respectively. A grey segment represents the fraction of residues that are not modelled. The numeric value for each fraction is indicated below the corresponding segment, with a dot representing fractions <=5% Note EDS was not executed.
Journal of Biomolecular NMR, 2010
We present a suite of software for the complete and easy deposition of NMR data to the PDB and BM... more We present a suite of software for the complete and easy deposition of NMR data to the PDB and BMRB. This suite uses the CCPN framework and introduces a freely downloadable, graphical desktop application called CcpNmr Entry Completion Interface (ECI) for the secure editing of experimental information and associated datasets through the lifetime of an NMR project. CCPN projects can be created within the CcpNmr Analysis software or by importing existing NMR data files using the CcpNmr FormatConverter. After further data entry and checking with the ECI, the project can then be rapidly deposited to the PDBe using AutoDep, or exported as a complete deposition NMR-STAR file. In full CCPN projects created with ECI, it is straightforward to select chemical shift lists, restraint data sets, structural ensembles and all relevant associated experimental collection details, which all are or will become mandatory when depositing to the PDB.
Glycobiology, 2000
of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 h... more of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 has been extended to include N-terminal domain amino acid residues 91-113 containing one of the nine proline-rich motifs present in full-length hamster galectin-3. The modeling predicts two configurations of the N-terminal tail: in one the tail turns toward the first (SI) and last (S12) β-strands of the CRD and lies at the apolar dimer interface observed for galectins-1 and-2. In the second folding arrangement the N-terminal tail lies across the carbohydrate-binding pocket of the CRD where it could participate in sugar-binding: in particular tyrosine 102 and adjacent residues may interact with the partly solvent exposed nonreducing N-acetylgalactosamine and fucose substituents of the A-blood group structure GalNAcα1,3 [Fucα1,2]Galβ1,4GlcNAc-R. Binding studies using surface plasmon resonance of a recombinant fragment ∆1-93 protein containing residues 94-245 of hamster galectin-3 and a collagenase-derived fragment ∆1-103 containing residues 104-245, as well as alanine mutagenesis of residues 101-105 in ∆1-93 protein, support the prediction that Tyr102 and adjacent residues make significant contributions to oligosaccharide binding.
Analytical Sciences, 1994
Acta Crystallographica Section A Foundations of Crystallography, 2006
MrBUMP is a new automated procedure for structure solution by Molecular Replacement. The aim of M... more MrBUMP is a new automated procedure for structure solution by Molecular Replacement. The aim of MrBUMP is to start from native structure factors and a target sequence, and deliver a positioned and partly refined model, suitable for further model rebuilding , model completion and/or refinement. In the highest level view, the process consists of three stages. In the first stage, the target sequence is used to search for related proteins in the Protein Data Bank. This gives a list of template chains, domains and multimers, which is passed to the search model preparation stage. Up to three search models are generated for each template, differing in the alignment used and the treatment of side chains. Finally, given a list of putative search models, a subset is passed to the MR stage which uses Phaser or Molrep. Initial restrained refinement of the positioned model is used to assess the putative solution. MrBUMP consists of a set of Python scripts which link together established programs. MrBUMP differs from other molecular replacement pipelines in two ways: Firstly, there is a greater emphasis on the discovery of potential search models. A list of search models is generated and many are tried in molecular replacement with the aim of finding the optimum model. Secondly, Mr Bump is intended for general use within the CCP4 software suite, and is designed to be portable and flexible. m03.o04
Acta Crystallographica Section A Foundations of Crystallography, 2005
As the throughput of X-ray diffraction laboratories increases and the groups of users diversify, ... more As the throughput of X-ray diffraction laboratories increases and the groups of users diversify, the need for an automatic report generation system becomes more apparent. Although the type of report varies depending on the user's objectives, the data in the report is always based on information gathered throughout the experiment. We present a relational database approach to report generation. For each step of the structure determination the relevant pieces of information are recorded, such as the type of operation, input and output data, software version, user name, date and time. Furthermore, by linking the input of an operation to the output of the preceding steps, each piece of information is put into context as and when it becomes available. From the emerging tree structure it is possible to create a report from the beginning of the experiment to any step in the experiment. Wrong paths that did not lead to the final result are preserved too. Reports come in different shapes and sizes: various formats (e.g. CIF, mmCIF, HTML, and proprietary formats), various purposes (e.g. publication, archiving, or visualization), and varying degrees of detail. In order to serve this wide spectrum of needs we have developed a template language that describes which data is extracted from the database and how it is formatted.
Acta Crystallographica Section A Foundations of Crystallography, 2002
Acta Crystallographica Section A Foundations of Crystallography, 1993
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, 1978
The complex forms centrosymmetric [(CH3)2T1]2(D-tryptophan)(L-tryptophan) dimers in which each TI... more The complex forms centrosymmetric [(CH3)2T1]2(D-tryptophan)(L-tryptophan) dimers in which each TI atom is bonded to one O atom and one N atom of an amino acid residue with the carboxyl group acting as a monodentate bridging group [TI-C = 2.11 (1), 2.12 (1); TI-O = 2.47 (I), 2.59 (1); TIN = 2.66 (1) AI. The coordination at the Tl atom is irregular and a vacant sixth coordination site is taken up by an essentially non-bonding contact (3.43 A) from the pyrrole N atom of a parallel dimer set. Adjacent dimers in the crystal are held together in polymeric chains by hydrogen bonding between the molecule of water of crystallization and the pyrrole N-H.
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, 1978
F(000) = 372. The complex, (CHa)2TI(L-PHE), in the crystal consists of two independent polymeric ... more F(000) = 372. The complex, (CHa)2TI(L-PHE), in the crystal consists of two independent polymeric chains of (CH3)2Tl(L-phenylalanine) units linked by the carboxyl groups [T1-C = 2-06 (2), 2.15 (2); TI-O = 2.65 (1), 2.63 (1); T1-N = 2-53 (1) and TI~-C = 2.17 (2), 2.09 (2); Tll-O = 2.66 (1), 2.54 (1); TP-N = 2.53 (1) A]. Each independent Tl atom is approximately octahedrally coordinated with the sixth coordination site in each case occupied by a bridging carboxyl O atom of an adjacent polymeric chain [T1-O = 3.13, 3.06 Al.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2012
The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. T... more The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. The structure of TRAP consists of a central eight-stranded β-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit.
Journal of the Chemical Society, Dalton Transactions, 1988
Sulphonic acids RSO3H (R = CH3, CF3, or C6H4CH3-p) react with the precursors [MH2(CO)(PPh3)3](M =... more Sulphonic acids RSO3H (R = CH3, CF3, or C6H4CH3-p) react with the precursors [MH2(CO)(PPh3)3](M = Ru or Os) and [Ru(CO)3(PPh3)2] or [OsH2(CO)2(PPh3)2] in refluxing benzene or toluene to afford the complexes [M(O3SR)2(H2O)(CO)(PPh3)2] and [M(O3SR)2(CO)2(PPh3)2] respectively. The precursors [RuH2(PPh3)4] and [OsH4(PPh3)3] react with sulphonic acids in refluxing benzene to give the η6-benzene complexes [MH(η6-C6H6)(PPh3)2][O3SR]. However a similar reaction in refluxing ethanol yielded [OsH3(PPh3)4][O3SCF3]. The complexes [Ru(O3SR)2(H2O)(CO)(PPh3)2] have been shown by variable-temperature 1H and 31P-{1H} n.m.r. spectroscopy to be fluxional in solution. The solid-state structure of one example, [Ru(O3SC6H4CH3-p)2(H2O)(CO)(PPh3)2] has been determined by X-ray diffraction methods. The crystals are monoclinic, space group P21/n, with a= 24.382(5), b= 18.075(4), c= 10.729(2)A, β= 99.03(2)°, and Z= 4. The octahedral ruthenium(II) complex contains monodentate sulphonate ligands (trans to PPh3 and CO) and an aqua ligand (trans to PPh3) with strong hydrogen-bonding interactions between the H atoms of the H2O and the non-co-ordinated oxygen atoms of the sulphonate ligands. The molecular structure is very similar to that previously reported for the alcohol dehydrogenation catalyst [Ru(O2CCF3)2(CH3OH)(CO)(PPh3)2].
Journal of the Chemical Society, Dalton Transactions, 1986
ABSTRACT
Journal of the Chemical Society, Chemical Communications, 1980
Journal of the Chemical Society, Dalton Transactions, 1990
Prolonged photolysis of [Mo2(η-C5H5)2(µ-H)(µ-PMe2)(CO)4] in the presence of allene gives the new ... more Prolonged photolysis of [Mo2(η-C5H5)2(µ-H)(µ-PMe2)(CO)4] in the presence of allene gives the new complexes [Mo2(η-C5H5)2{µ-η5-CH2C(CH2)C(Me)CH2}(µ-PMe2)(CO)2] and [Mo2(η-C5H5)2(µ-PMe2){η3-CH2C(CH2)C(Me)CH2}(CO)3] the structures of which in the solid state have been determined by single-crystal X-ray analyses. The former of these new complexes is also obtained in the reaction of the µ-vinyl complex [Mo2(η-C5H5)2{µ-σ:η2-C(Me)CH2}(µ-PMe2)(CO)3] with allene but not in the reaction of the isomeric η3-allyl complex [Mo2(η-C5H5)2(µ-PMe2)-(η3-C3H5)(CO)3] with allene. On the other hand the syn-methylallyl complex [Mo(η-C5H5)2(µ-PMe2)(η3-syn-MeCHCH2CH2)(CO)3] does react with allene to give a ca. 1:2 inseparable mixture of [Mo2(η-C5H5)2{µ-η5-CH2C(CH2)C(Me)CHMe}(µ-PMe2)(CO)2] and [Mo2(η-C5H6)2{µσ:η5-CH2C(CH2)C(Et)CH2}(µ-PMe2)(CO)2]. These complexes may be obtained separately from reactions of the appropriate µ-vinyl complexes with allene. The mechanism of formation of the new complexes is discussed in the light of the above experimental results.
Journal of the Chemical Society, Dalton Transactions, 1984
The chlorohydridorhodium(III) complex of (o-diphenylphosphinophenyl)amine, [RhH(NH2C6H4PPh2-o)2Cl... more The chlorohydridorhodium(III) complex of (o-diphenylphosphinophenyl)amine, [RhH(NH2C6H4PPh2-o)2Cl]Cl (1a), formed by oxidative addition of HCl to [Rh(NH2C6H4PPh2-o)2]BF4(2b), was found to react with air to give two products. These have been characterised by X-ray structure analysis as the cis-dichloro-complex [Rh(NH2C6H4PPh2-o)(NHC6H4PPh2-o)Cl2](6), containing an amino- and amido-donor group, and the trans-dichloro-complex [Rh(NH2C6H4PPh2-o)2Cl2][p-MeC6H4SO3](8). Crystals of (6) are monoclinic, space group P21/n, with a= 17.153(3), b= 18.667(3), c= 9.891(2)A, β= 91.77(3)°, and Z= 4. Blocked full-matrix refinement using 3 501 unique data [I 3σ(I), 3 ⩽θ⩽ 25°] gave R= 0.0487, R′= 0.0511. Complex (8) crystallises, with a molecule of acetonitrile as solvate, in the monoclinic space group I2/c with a= 18.394(4), b= 14.380(3), c= 16.378(3)A, β= 96.67(4)°, and Z= 4. Blocked full-matrix refinement of 2 741 reflections with I 3σ(I)(3 ⩽θ⩽ 25°) gave R= 0.0638 and R′= 0.0698. The cation of (8) has exact C2 symmetry. A mechanism for the reaction is proposed which involves peroxo- and hydrogenperoxo-species.
Journal of the Chemical Society, Chemical Communications, 1982
ABSTRACT
Journal of the Chemical Society, Chemical Communications, 1980
ABSTRACT