Complex formation between methionine and a heme peptide from cytochrome c. - Wikidata - awgldk - TriplyDB

Complex formation between methionine and a heme peptide from cytochrome c.

Complex formation between methionine and a heme peptide from cytochrome c.

http://www.wikidata.org/entity/Q34421175

about

Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase Resolving the individual components of a pH-induced conformational change.Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Binding of imidazole to the heme of cytochrome c1 and inhibition of the bc1 complex from Rhodobacter sphaeroides: II. Kinetics and mechanism of binding Gaussian fluctuations and linear response in an electron transfer protein.Effects of nonpolar environments on the redox potentials of heme complexes.Semisynthetic cytochrome c.Proton magnetic resonance spectra of Rhodospirillum rubrum cytochrome c2 High-resolution proton nuclear magnetic resonance spectroscopy of cytochrome.The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.Porphyrin-binding proteins in serum.Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine residue 65 Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center.Conformational changes in hemoproteins of the respiratory chain.Simulation of electron-proton coupling with a Monte Carlo method: application to cytochrome c3 using continuum electrostatics.Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels.Modification of methionine in the haem environment of cytochrome c.Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Chemistry of type c heme-peptide systems.

P2860

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P2860

Complex formation between methionine and a heme peptide from cytochrome c.

http://www.wikidata.org/entity/Q34421175

description

1965 nî lūn-bûn

@nan

1965 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1965 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

1965年の論文

@ja

1965年論文

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1965年論文

@zh-hant

1965年論文

@zh-hk

1965年論文

@zh-mo

1965年論文

@zh-tw

1965年论文

@wuu

name

Complex formation between methionine and a heme peptide from cytochrome c.

@ast

Complex formation between methionine and a heme peptide from cytochrome c.

@en

Complex formation between methionine and a heme peptide from cytochrome c.

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type

label

Complex formation between methionine and a heme peptide from cytochrome c.

@ast

Complex formation between methionine and a heme peptide from cytochrome c.

@en

Complex formation between methionine and a heme peptide from cytochrome c.

@nl

prefLabel

Complex formation between methionine and a heme peptide from cytochrome c.

@ast

Complex formation between methionine and a heme peptide from cytochrome c.

@en

Complex formation between methionine and a heme peptide from cytochrome c.

@nl

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Complex formation between methionine and a heme peptide from cytochrome c.

@en

P2093

Cronin JR

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Fanger MW

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Harbury HA

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Hettinger TP

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Murphy AJ

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Myer YP

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Vinogradov SN

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P2860

GUANIDINATED CYTOCHROME C.

LINKED FUNCTIONS IN HEME SYSTEMS: OXIDATION-REDUCTION POTENTIALS AND ABSORPTION SPECTRA OF A HEME PEPTIDE OBTAINED UPON PEPTIC HYDROLYSIS OF CYTOCHROME C

A study of the cytochrome c haemochromogen.

THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551.

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1658-1664

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scholarly article

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10.1073/PNAS.54.6.1658

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6

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54

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1965-12-01T00:00:00Z

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