Engineering the Substrate Specificity and Reactivity of a Heme Protein: Creation of an Ascorbate Binding Site in Cytochrome c Peroxidase † (original ) (raw )Evaluating the Roles of the Heme a Side Chains in Cytochrome c Oxidase Using Designed Heme Proteins †
宗挺 王
Biochemistry, 2006
View PDFchevron_right
Altering Substrate Specificity at the Heme Edge of Cytochrome c Peroxidase †
Duncan McRee
Biochemistry, 1996
View PDFchevron_right
Posttranslational modification of heme in peroxidases - Impact on structure and catalysis
Markus Auer
Archives of biochemistry and biophysics, 2018
View PDFchevron_right
Iron Oxidation State Modulates Active Site Structure in a Heme Peroxidase † , ‡
Peter Moody
Biochemistry, 2008
View PDFchevron_right
Evidence for Heme Oxygenase Activity in a Heme Peroxidase
Peter Moody
Biochemistry, 2009
View PDFchevron_right
How Cytochromes with Different Folds Control Heme Redox Potentials
Karin Hauser
Biochemistry, 2003
View PDFchevron_right
The role of the heme propionates in heme biochemistry
Victor Guallar
Journal of Inorganic Biochemistry, 2006
View PDFchevron_right
Conformational Mobility in the Active Site of a Heme Peroxidase
Peter Moody
Journal of Biological Chemistry, 2006
View PDFchevron_right
Coupled Oxidation vs Heme Oxygenation: Insights from Axial Ligand Mutants of Mitochondrial Cytochrome b5
Mario Rivera
Journal of the American Chemical Society, 2003
View PDFchevron_right
Heme–heme communication during the alkaline-induced structural transition in cytochrome c oxidase
Syunru Yeh
Journal of Inorganic Biochemistry, 2008
View PDFchevron_right
Conversion of Mitochondrial Cytochrome b5 into A Species Capable of Performing the Efficient Coupled Oxidation of Heme
Juan Carlos Rodriguez
Biochemistry, 1998
View PDFchevron_right
The Reduction Potential of Cytochrome b 5 Is Modulated by Its Exposed Heme Edge
Mario Rivera
Biochemistry, 1998
View PDFchevron_right
A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase
Colin Levy
JACS Au, 2021
View PDFchevron_right
The dynamic role of distal side residues in heme hydroperoxidase catalysis. Interplay between X-ray crystallography and ab initio MD simulations
Mercedes Alfonso-Prieto
Archives of Biochemistry and Biophysics, 2010
View PDFchevron_right
Heme oxygenation and the widening paradigm of heme degradation
Geoffrey Heinzl
Archives of Biochemistry and Biophysics, 2014
View PDFchevron_right
Disruption of an Active Site Hydrogen Bond Converts Human Heme Oxygenase1 into a Peroxidase
Luke Lightning
Journal of Biological Chemistry, 2001
View PDFchevron_right
A Novel Heme and Peroxide-dependent Tryptophan–tyrosine Cross-link in a Mutant of Cytochrome c Peroxidase
Chad Immoos
Journal of Molecular Biology, 2003
View PDFchevron_right
The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE
Takeshi Uchida
Journal of Biological Chemistry, 2004
View PDFchevron_right
Heme-heme interaction in cytochrome oxidase
John G O R D O N Lindsay
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
View PDFchevron_right
How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase
Georg Schütz , Markus Auer
The Journal of biological chemistry, 2014
View PDFchevron_right
The heme regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation
Stephen Ragsdale
Journal of Biological Chemistry, 2020
View PDFchevron_right
Structure and Reaction Mechanism in the Heme Dioxygenases
Sandeep Handa
Biochemistry, 2011
View PDFchevron_right
Explaining the Atypical Reaction Profiles of Heme Enzymes with a Novel Mechanistic Hypothesis and Kinetic Treatment
binoy mathew
PLOS One, 2010
View PDFchevron_right
Cytochrome c Peroxidase Complexed with Cytochrome c Has an Unperturbed Heme Moiety †
Mark Ondrias
Biochemistry, 1996
View PDFchevron_right
Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase
Thomas Spiro
Biochemistry, 1991
View PDFchevron_right
The Protein Effect in the Structure of Two Ferryl-Oxo Intermediates at the Same Oxidation Level in the Heme Copper Binuclear Center of Cytochrome c Oxidase
Constantinos Varotsis
Journal of Biological Chemistry, 2013
View PDFchevron_right
Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?
Marten Vos
Proceedings of the National Academy of Sciences, 2000
View PDFchevron_right
An Arginine to Lysine Mutation in the Vicinity of the Heme Propionates Affects the Redox Potentials of the Hemes and Associated Electron and Proton Transfer in Cytochrome c Oxidase †
Lois Geren
Biochemistry, 2005
View PDFchevron_right
HEMES REVISITED BY DENSITY FUNCTIONAL APPROACHES. 2. A PARADIGM FOR AXIAL LIGATION IN HEMOPROTEINS
Radu Silaghi-Dumitrescu
View PDFchevron_right
Site-directed mutagenesis of tetraheme cytochrome c3: Modification of oxidoreduction potentials after heme axial ligand replacement
Isabelle Mus-Veteau
Journal of Biological Chemistry
View PDFchevron_right