Results 231 to 240 of about 279,218 (267)

The reactivity of thiol groups in bovine heart cytochrome c oxidase towards 5,5′-dithiobis(2-nitrobenzoic acid)

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
Bovine heart cytochrome c oxidase consists of 12 stoicheiometric polypeptide chains of at least 11 different types. The enzyme contains 14--16 cysteine residues; the distribution of nearly all cysteine residues over the subunits has been established.
F E, Verheul, J W, Draijer, A O, Muijsers, B F, Van Gelder   +3 more
openaire   +2 more sources

The pH dependence of the stereochemistry around the heme group in NO–cytochrome c (horse heart)

Inorganica Chimica Acta, 1988
The electronic absorption, EPR and MCD spectra of NO derivatives of both ferrous and ferric cytochrome c (horse heart) have been measured in the pH region 2.0 to 12.9, in order to elucidate the pH dependence of the stereochemistry around the heme group.
Tetsushiko Yoshimura, Shinnichiro Suzuki
openaire   +1 more source

1H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Abstract Cytochrome c-555 from Chlorobium thiosulfatophilum was investigated by 1H nuclear magnetic resonance at 360 MHz. Individual 1H-NMR assignments were obtained for heme c, and the side-chain proton resonances of the axial methionine and the imidazole ring proton lines of the axial histidine were identified.
Hans Senn, Michael A. Cusanovich, Kurt Wüthrich   +2 more
openaire   +1 more source

Spectroscopic Properties of a Mitochondrial Cytochromecwith a Single Thioether Bond to the Heme Prosthetic Group

Biochemistry, 2002
The yeast iso-1-cytochrome c variant Cys14Ser has been prepared in which one of the two thioether bonds by which the heme prosthetic group is normally bound to the protein has been eliminated. Comparison of the properties of this variant with those of the wild-type cytochrome provides insight into the role of this covalent attachment of the heme group ...
Federico I, Rosell, A Grant, Mauk
openaire   +2 more sources

Reactive Amino Groups in Baker's Yeast Cytochrome c

The Journal of Biochemistry, 1966
C, Sato, K, Titani, K, Narita
openaire   +2 more sources

Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c

Biochemistry, 1983
F, Millett, C, de Jong, L, Paulson, R A, Capaldi   +3 more
openaire   +2 more sources

REACTIVITY OF THIOL GROUPS IN CYTOCHROME c OXIDASE

Biochemical Society Transactions, 1981
F. E. A. M. Verheul, J. W. Draijer, I. K. Dentener, A. O. Muijsers   +3 more
openaire   +1 more source

Modification of carboxyl groups on NADPH-cytochrome P-450 reductase involved in binding of cytochromes c and P-450 LM2.

Biochemistry international, 1988
Carboxyl groups of NADPH-cytochrome P-450 reductase have been modified with the water-soluble carbodiimide EDC. Although there is no significant loss in DCPIP reduction the activity with cytochrome c and cytochrome P-450 LM2 as electron acceptors was inhibited by about 60 and 85%, respectively (1 h incubation time, 20 mM EDC).
R, Bernhardt, K, Pommerening, K, Ruckpaul   +2 more
openaire   +1 more source

MULTIPLE PROSTHETIC GROUPS IN CYTOCHROME C

Journal of the American Chemical Society, 1954
M. Morrison, R. W. Estabrook, E. Stotz
openaire   +1 more source

Pseudomonas Cytochrome c. I. Effect of Modification of the Amino Groups^*

Biochemistry, 1967
S N, Vinogradov, H A, Harbury
openaire   +2 more sources