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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30 September 2019

A Warshel

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30 September 2019

Geoffrey Robert Moore

object named as

G R Moore

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30 September 2019

R L Cutler

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30 September 2019

A M Davies

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30 September 2019

S Creighton

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M Smith

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A G Mauk

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30 September 2019

language of work or name

English

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publication date

1 April 1989

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30 September 2019

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volume

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issue

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30 September 2019

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

cites work

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Sequence of the gene for iso-l-cytochrome c in saccharomyces cerevisiae

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Control of redox properties of cytochrome c by special electrostatic interactions

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Rapid and efficient site-specific mutagenesis without phenotypic selection

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Free energy of charges in solvated proteins: microscopic calculations using a reversible charging process

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Calculations of electrostatic interactions in biological systems and in solutions

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

The conformation of eukaryotic cytochrome c around residues 39, 57, 59 and 74.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

A new non-covalent complex of semisynthetically modified tryptic fragments of cytochrome c.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

2 New M13 vectors for cloning

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Factors influencing redox potentials of electron transfer proteins

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Semisynthesis of cytochrome c analogues. The effect of modifying the conserved residues 38 and 39.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Structural basis for the variation in redox potential of cytochromes

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Toward computer-aided site-directed mutagenesis of enzymes

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Solution structure of mitochondrial cytochrome c. II. 1H nuclear magnetic resonance of ferrocytochrome c

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Yeast iso-1-cytochrome c. A 2.8 A resolution three-dimensional structure determination

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

A denaturation-induced proton-uptake study of horse ferricytochrome c.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Preparation of cytochrome c peroxidase from baker's yeast

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Effects of Nonpolar Environments on the Redox Potentials of Heme Complexes

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Structural basis for the variation of pH-dependent redox potentials of Pseudomonas cytochromes c-551

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Determination of the coordination geometry at the heme iron in three cytochromes c from Saccharomyces cerevisiae and from Candida krusei based on individual 1H-NMR assignments for heme c and the axially coordinated amino acids

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Oligonucleotide-Directed Mutagenesis: A Simple Method Using Two Oligonucleotide Primers and a Single-Stranded DNA Template

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

The gapped duplex DNA approach to oligonucleotide-directed mutation construction.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1021/BI00434A012

Identifiers

DOI

10.1021/BI00434A012

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30 September 2019

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