ChemInform Abstract: SPECIES SPECIFICITY OF LONG-RANGE ELECTRON TRANSFER WITHIN THE COMPLEX BETWEEN ZINC-SUBSTITUTED CYTOCHROME C PEROXIDASE AND CYTOCHROME C

1985 ◽  
Vol 16 (27) ◽  
Author(s):  
P. S. HO ◽  
C. SUTORIS ◽  
N. LIANG ◽  
E. MARGOLIASH ◽  
B. M. HOFFMAN
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Long Range ◽  
Cytochrome C Peroxidase ◽  
Species Specificity

Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

Science ◽  
1988 ◽  
Vol 240 (4850) ◽  
pp. 311-313 ◽  
Author(s):  
N Liang ◽  
AG Mauk ◽  
GJ Pielak ◽  
JA Johnson ◽  
M Smith ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Long Range ◽  
Transfer Process ◽  
Cytochrome C Peroxidase ◽  
Electron Transfer Process ◽  
Aromatic Residues ◽  
Transfer Step

Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is approximately 10(4) slower at approximately 0 degrees C than for the two variants with aromatic residues.

In Silico Spectroscopy of Tryptophan and Tyrosine Radicals Involved in the Long-Range Electron Transfer of Cytochrome c Peroxidase

2014 ◽  
Vol 118 (32) ◽  
pp. 9525-9537 ◽  
Author(s):  
Caterina Bernini ◽  
Elena Arezzini ◽  
Riccardo Basosi ◽  
Adalgisa Sinicropi
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Long Range ◽  
In Silico ◽  
Cytochrome C Peroxidase

Long-range electron transfer from iron(II)-cytochrome c to (zinc-cytochrome c peroxidase)(+) within the 1:1 complex

1986 ◽  
Vol 108 (15) ◽  
pp. 4665-4666 ◽  
Author(s):  
Nong. Liang ◽  
Chae Hee. Kang ◽  
E. Margoliash ◽  
Pui Shing. Ho ◽  
Brian M. Hoffman
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Long Range ◽  
Cytochrome C Peroxidase

Multiphasic intracomplex electron transfer from cytochrome c to zinc cytochrome c peroxidase: conformational control of reactivity

1991 ◽  
Vol 113 (5) ◽  
pp. 1842-1844 ◽  
Author(s):  
Sten A. Wallin ◽  
Eric D. A. Stemp ◽  
Andrew M. Everest ◽  
Judith M. Nocek ◽  
Thomas L. Netzel ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Conformational Control

Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II

Biochemistry ◽  
1994 ◽  
Vol 33 (29) ◽  
pp. 8678-8685 ◽  
Author(s):  
Rui-Qin Liu ◽  
Mark A. Miller ◽  
Gye Won Han ◽  
Seung Hahm ◽  
Lois Geren ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Intramolecular Electron Transfer ◽  
Compound Ii
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