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Papers by Jane Vanderkooi
Biochimica Et Biophysica Acta - Biomembranes, 1977
Biochimica et biophysica acta, Sep 1, 1977
Biochemistry, Jun 1, 1990
Proceedings of SPIE, Apr 1, 1992
ABSTRACT
Chemical Physics, Dec 1, 1997
Abstract We performed hole burning Stark effect experiments on a cytochrome c type protein. From ... more Abstract We performed hole burning Stark effect experiments on a cytochrome c type protein. From the behavior of the holes in an external electric field conclusions on local electric fields in the heme pocket can be drawn. We varied the pH value in order to study the influence of different groups on the pocket field: (a) titratable amino acid residues, (b) the porphyrin side chains (especially the propionates) and (c) the two axial ligands His18 and Met80. Surprisingly, a variation of the pH between 4.1 and 12.7 has no influence on the Stark effect. However, at a pH-level
Biophysical Journal, Sep 1, 1998
Biochemistry, Jun 27, 1989
Biochemistry, 1996
ABSTRACT
Biochemistry, Dec 1, 1997
The carboxylate groups of organic acids give strong absorption in the infrared between approximat... more The carboxylate groups of organic acids give strong absorption in the infrared between approximately 1550 and 1650 cm-1. For acetate and chloroacetate derivatives, the infrared (IR) frequency of the carboxylate antisymmetric stretching mode (v(a)OCO) is related to the square root of the pK of the acid, with a shift of approximately 20 cm-1 to higher frequency for a pK drop in the range 5-3. It follows that v(a)OCO may respond to conditions on the protein surface. In this paper, the IR amide I' and carboxylate absorptions of cytochrome c from horse, yeast, and tuna are compared with model compounds such as Val-Glu and microperoxidase-11, the 11 amino acid fragment of horse cytochrome c containing the covalently bound heme. For microperoxidase-11, the contribution from all four carboxylates can be accounted for and the 1567 cm-1 absorption is assigned to the heme propionates. For the proteins, the carboxylate absorption band is inhomogeneous, i.e., there is a distribution of frequencies. Both the amide I' and carboxylate bands are sensitive to protein conformation as shown by their different pH, salt, and redox dependence.
Biophysical Journal, Jun 1, 1995
Biophysical Journal, Mar 1, 2002
Archives of Biochemistry and Biophysics, May 1, 1971
Abstract The enhancement of the fluorescence of 8-anilino-1-naphthalene sulfonic acid (ANS) by sk... more Abstract The enhancement of the fluorescence of 8-anilino-1-naphthalene sulfonic acid (ANS) by skeletal muscle microsomes is dependent upon the cation concentration of the medium. The accumulation of Ca 2+ by microsomes in systems containing Ca-EGTA buffer, MgCl 2 (0.1–3.0 m m ) and ATP (0.001–1 m m ), ITP, acetylphosphate, or carbamylphosphate as energy donors, is reflected in enhanced ANS fluorescence. The fluorescence is reduced parallel with the release of Ca 2+ on the addition of Salyrgan or after ATP is depleted. Fluorescence increase was found when Ca 2+ was replaced with Sr 2+ but not with Mn, Cd. or Ba. Glyceraldehyde-3-phosphate, IDP, ADP, inorganic triphosphate, pyrophosphate, and orthophosphate, were ineffective as energy donors. Addition of 3 m m oxalate to Ca 2+ -loaded microsomes decreased the fluorescence intensity. These results are consistent with the view that the fluorescence enhancement during Ca 2+ accumulation results from changes in the environment of the dye caused by the binding of actively transported Ca 2+ to the membrane.
Biochemistry, Mar 25, 1998
Biochimica Et Biophysica Acta - Bioenergetics, Aug 1, 1989
Overview of factors influencing the appearance and disappearance of the triplet state molecule . ... more Overview of factors influencing the appearance and disappearance of the triplet state molecule . . . 3 A. Population of the triplet state . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3 B. Phosphorescence decay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3 C. Delayed fluorescence . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4 D. Quenching by neighboring molecules . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5 E. Influence of diffusion on quenching . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5
Archives of Biochemistry and Biophysics, Dec 1, 1971
Abstract The Ca permeability of phosphatidyl choline vesicles of diverse fatty acid composition w... more Abstract The Ca permeability of phosphatidyl choline vesicles of diverse fatty acid composition was measured. The rate of 45 Ca release from liposomes equilibrated with 1 m m 45 CaCl 2 was found to be about 8 × 10 −18 moles of Ca/cm 2 /sec for egg lecithin and about 5.3 × 10 −17 moles of Ca/cm 2 /sec for dioleyllecithin at 30 °. Incorporation of cholesterol into dioleyllecithin micelles reduced the rate of Ca release. The Ca permeability of the phosphatidyl choline micelles was insensitive to changes in the pH, calcium or sodium concentration of the medium but increased with increasing temperature. The effect of temperature was most marked with dioleyl lecithin dispersions, but was clearly apparent with dipalmitoyl, plant, bovine, and egg lecithins as well. The activation energy of Ca release fell in the range of 4.2–9.6 kcal/mole. Macrocyclic antibiotics (valinomycin, tyrocidin, and gramicidin) at relatively high concentration increased the rate of Ca release similarly to their effects on fragmented sarcoplasmic reticulum membranes.
Accounts of Chemical Research, Oct 21, 2009
European journal of biochemistry, Dec 1, 1975
A cytochrome c derivative from which iron is removed has been prepared and characterized. Several... more A cytochrome c derivative from which iron is removed has been prepared and characterized. Several lines of evidence indicate that native and porphyrin cytochrome c have similar conformations: they have similar elution characteristics on Sephadex gel chromatography; in both proteins the tryptophan fluorescence is quenched and the pK values of protonation of the porphyrin are identical. Porphyrin cytochrome c does not substitute for native cytochrome c in either the oxidase reaction or in restoring electron transport in cytochrome-c-depleted mitochondria. It does however competitively inhibit native cytochrome c in these reactions, the Ki for inhibition being larger than the Km for reaction. The absorption and emission spectra, and the polarized excitation spectrum of the porphyrin cytochrome c are characteristic of free base porphyrin. The absence of fluorescence quenching of porphyrin cytochrome c when the protein is bound to cytochrome oxidase suggests that heme to heme distance between these proteins is larger than 0.5 to 0.9 nm depending upon orientation. Binding of the porphyrin cytochrome c to phospholipids or to mitochondria increases the fluorescence polarization of a positively polarized absorption band, which indicates that the bound form of the protein does not rotate freely within the time scale of relaxation from the excited state.
Physics Today, Feb 1, 1995
Biochimica Et Biophysica Acta - Biomembranes, 1977
Biochimica et biophysica acta, Sep 1, 1977
Biochemistry, Jun 1, 1990
Proceedings of SPIE, Apr 1, 1992
ABSTRACT
Chemical Physics, Dec 1, 1997
Abstract We performed hole burning Stark effect experiments on a cytochrome c type protein. From ... more Abstract We performed hole burning Stark effect experiments on a cytochrome c type protein. From the behavior of the holes in an external electric field conclusions on local electric fields in the heme pocket can be drawn. We varied the pH value in order to study the influence of different groups on the pocket field: (a) titratable amino acid residues, (b) the porphyrin side chains (especially the propionates) and (c) the two axial ligands His18 and Met80. Surprisingly, a variation of the pH between 4.1 and 12.7 has no influence on the Stark effect. However, at a pH-level
Biophysical Journal, Sep 1, 1998
Biochemistry, Jun 27, 1989
Biochemistry, 1996
ABSTRACT
Biochemistry, Dec 1, 1997
The carboxylate groups of organic acids give strong absorption in the infrared between approximat... more The carboxylate groups of organic acids give strong absorption in the infrared between approximately 1550 and 1650 cm-1. For acetate and chloroacetate derivatives, the infrared (IR) frequency of the carboxylate antisymmetric stretching mode (v(a)OCO) is related to the square root of the pK of the acid, with a shift of approximately 20 cm-1 to higher frequency for a pK drop in the range 5-3. It follows that v(a)OCO may respond to conditions on the protein surface. In this paper, the IR amide I' and carboxylate absorptions of cytochrome c from horse, yeast, and tuna are compared with model compounds such as Val-Glu and microperoxidase-11, the 11 amino acid fragment of horse cytochrome c containing the covalently bound heme. For microperoxidase-11, the contribution from all four carboxylates can be accounted for and the 1567 cm-1 absorption is assigned to the heme propionates. For the proteins, the carboxylate absorption band is inhomogeneous, i.e., there is a distribution of frequencies. Both the amide I' and carboxylate bands are sensitive to protein conformation as shown by their different pH, salt, and redox dependence.
Biophysical Journal, Jun 1, 1995
Biophysical Journal, Mar 1, 2002
Archives of Biochemistry and Biophysics, May 1, 1971
Abstract The enhancement of the fluorescence of 8-anilino-1-naphthalene sulfonic acid (ANS) by sk... more Abstract The enhancement of the fluorescence of 8-anilino-1-naphthalene sulfonic acid (ANS) by skeletal muscle microsomes is dependent upon the cation concentration of the medium. The accumulation of Ca 2+ by microsomes in systems containing Ca-EGTA buffer, MgCl 2 (0.1–3.0 m m ) and ATP (0.001–1 m m ), ITP, acetylphosphate, or carbamylphosphate as energy donors, is reflected in enhanced ANS fluorescence. The fluorescence is reduced parallel with the release of Ca 2+ on the addition of Salyrgan or after ATP is depleted. Fluorescence increase was found when Ca 2+ was replaced with Sr 2+ but not with Mn, Cd. or Ba. Glyceraldehyde-3-phosphate, IDP, ADP, inorganic triphosphate, pyrophosphate, and orthophosphate, were ineffective as energy donors. Addition of 3 m m oxalate to Ca 2+ -loaded microsomes decreased the fluorescence intensity. These results are consistent with the view that the fluorescence enhancement during Ca 2+ accumulation results from changes in the environment of the dye caused by the binding of actively transported Ca 2+ to the membrane.
Biochemistry, Mar 25, 1998
Biochimica Et Biophysica Acta - Bioenergetics, Aug 1, 1989
Overview of factors influencing the appearance and disappearance of the triplet state molecule . ... more Overview of factors influencing the appearance and disappearance of the triplet state molecule . . . 3 A. Population of the triplet state . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3 B. Phosphorescence decay . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3 C. Delayed fluorescence . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4 D. Quenching by neighboring molecules . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5 E. Influence of diffusion on quenching . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5
Archives of Biochemistry and Biophysics, Dec 1, 1971
Abstract The Ca permeability of phosphatidyl choline vesicles of diverse fatty acid composition w... more Abstract The Ca permeability of phosphatidyl choline vesicles of diverse fatty acid composition was measured. The rate of 45 Ca release from liposomes equilibrated with 1 m m 45 CaCl 2 was found to be about 8 × 10 −18 moles of Ca/cm 2 /sec for egg lecithin and about 5.3 × 10 −17 moles of Ca/cm 2 /sec for dioleyllecithin at 30 °. Incorporation of cholesterol into dioleyllecithin micelles reduced the rate of Ca release. The Ca permeability of the phosphatidyl choline micelles was insensitive to changes in the pH, calcium or sodium concentration of the medium but increased with increasing temperature. The effect of temperature was most marked with dioleyl lecithin dispersions, but was clearly apparent with dipalmitoyl, plant, bovine, and egg lecithins as well. The activation energy of Ca release fell in the range of 4.2–9.6 kcal/mole. Macrocyclic antibiotics (valinomycin, tyrocidin, and gramicidin) at relatively high concentration increased the rate of Ca release similarly to their effects on fragmented sarcoplasmic reticulum membranes.
Accounts of Chemical Research, Oct 21, 2009
European journal of biochemistry, Dec 1, 1975
A cytochrome c derivative from which iron is removed has been prepared and characterized. Several... more A cytochrome c derivative from which iron is removed has been prepared and characterized. Several lines of evidence indicate that native and porphyrin cytochrome c have similar conformations: they have similar elution characteristics on Sephadex gel chromatography; in both proteins the tryptophan fluorescence is quenched and the pK values of protonation of the porphyrin are identical. Porphyrin cytochrome c does not substitute for native cytochrome c in either the oxidase reaction or in restoring electron transport in cytochrome-c-depleted mitochondria. It does however competitively inhibit native cytochrome c in these reactions, the Ki for inhibition being larger than the Km for reaction. The absorption and emission spectra, and the polarized excitation spectrum of the porphyrin cytochrome c are characteristic of free base porphyrin. The absence of fluorescence quenching of porphyrin cytochrome c when the protein is bound to cytochrome oxidase suggests that heme to heme distance between these proteins is larger than 0.5 to 0.9 nm depending upon orientation. Binding of the porphyrin cytochrome c to phospholipids or to mitochondria increases the fluorescence polarization of a positively polarized absorption band, which indicates that the bound form of the protein does not rotate freely within the time scale of relaxation from the excited state.
Physics Today, Feb 1, 1995