Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium (Q69351795)

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30 September 2019

title

Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium (English)

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4

A Warshel

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30 September 2019

Geoffrey Robert Moore

5

object named as

G R Moore

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30 September 2019

author name string

R L Cutler

1

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A M Davies

2

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S Creighton

3

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M Smith

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A G Mauk

7

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language of work or name

English

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publication date

1 April 1989

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volume

28

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issue

8

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page(s)

3188-3197

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Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins.

30 September 2019

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Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants

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Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein

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Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems

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The semisynthesis of analogues of cytochrome c. Modifications of arginine residues 38 and 91

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Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by penta

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Effects of Nonpolar Environments on the Redox Potentials of Heme Complexes

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Identifiers

DOI

10.1021/BI00434A012

1 reference

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30 September 2019

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