THE PROTEIN MOIETY MODULATES THE REDOX POTENTIAL IN CYTOCHROMES-C

被引：46

作者：

DOLLA, A

BLANCHARD, L

GUERLESQUIN, F

BRUSCHI, M

机构：

[1] Unité de Bioénergétique et Ingénierie des Protéines, CNRS

来源：

BIOCHIMIE | 1994年 / 76卷 / 06期

关键词：

CYTOCHROME C; REDOX POTENTIAL; OXIDOREDUCTION PROTEINS;

D O I：

10.1016/0300-9084(94)90171-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cytochrome c is one of the most thoroughly documented oxidoreduction proteins. Its electron transfer activity, which involves an association between the heme group and the polypeptidic chain, is correlated with the redox potential value of the heme group. The redox potential covers a wide range up to 0.8 V, an extreme case being observed in the low-potential cytochromes c from sulfate reducing bacteria. One of the main roles of the polypeptidic moiety consists of modulating the redox potential value of the heme group. In this paper, some structural factors that seem likely to be involved in maintaining the redox potential value are described.

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收藏

页码：471 / 479

页数：9

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[1] SEQUENCE VARIABILITY IN BACTERIAL CYTOCHROMES-C [J].

AMBLER, RP .

BIOCHIMICA ET BIOPHYSICA ACTA, 1991, 1058 (01) :42-47

[2] MOLECULAR-STRUCTURE OF CYTOCHROME-C2 ISOLATED FROM RHODOBACTER-CAPSULATUS DETERMINED AT 2.5-A RESOLUTION [J].

BENNING, MM ;

WESENBERG, G ;

CAFFREY, MS ;

BARTSCH, RG ;

MEYER, TE ;

CUSANOVICH, MA ;

RAYMENT, I ;

HOLDEN, HM .

JOURNAL OF MOLECULAR BIOLOGY, 1991, 220 (03) :673-685

[3]

BLANCHARD L, 1994, IN PRESS EUR J BIOCH

[4] STRUCTURALLY ENGINEERED CYTOCHROMES WITH NOVEL LIGAND-BINDING SITES - OXY AND CARBONMONOXY DERIVATIVES OF SEMISYNTHETIC HORSE HEART ALA80 CYTOCHROME-C [J].

BREN, KL ;

GRAY, HB .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (22) :10382-10383

[5] THE PRIMARY STRUCTURE OF THE TETRAHEM CYTOCHROME-C3 FROM DESULFOVIBRIO-DESULFURICANS (STRAIN NORWAY-4) - DESCRIPTION OF A NEW CLASS OF LOW-POTENTIAL CYTOCHROME-C [J].

BRUSCHI, M .

BIOCHIMICA ET BIOPHYSICA ACTA, 1981, 671 (02) :219-226

[6] BIOCHEMICAL AND SPECTROSCOPIC CHARACTERIZATION OF THE HIGH-MOLECULAR-WEIGHT CYTOCHROME-C FROM DESULFOVIBRIO-VULGARIS HILDENBOROUGH EXPRESSED IN DESULFOVIBRIO-DESULFURICANS G200 [J].

BRUSCHI, M ;

BERTRAND, P ;

MORE, C ;

LEROY, G ;

BONICEL, J ;

HALADJIAN, J ;

CHOTTARD, G ;

POLLOCK, WBR ;

VOORDOUW, G .

BIOCHEMISTRY, 1992, 31 (12) :3281-3288

[7] IMPORTANCE OF A CONSERVED HYDROGEN-BONDING NETWORK IN CYTOCHROMES-C TO THEIR REDOX POTENTIALS AND STABILITIES [J].

CAFFREY, MS ;

DALDAL, F ;

HOLDEN, HM ;

CUSANOVICH, MA .

BIOCHEMISTRY, 1991, 30 (17) :4119-4125

[8] ROLE OF THE HIGHLY CONSERVED TRYPTOPHAN OF CYTOCHROME-C IN STABILITY [J].

CAFFREY, MS ;

CUSANOVICH, MA .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1993, 304 (01) :205-208

[9] THE AMINO-ACID SEQUENCE OF LOW-POTENTIAL CYTOCHROME-C550 FROM THE CYANOBACTERIUM MICROCYSTIS-AERUGINOSA [J].

COHN, CL ;

SPRINKLE, JR ;

ALAM, J ;

HERMODSON, M ;

MEYER, T ;

KROGMANN, DW .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1989, 270 (01) :227-235

[10] ROLE OF ARGININE-38 IN REGULATION OF THE CYTOCHROME-C OXIDATION-REDUCTION EQUILIBRIUM [J].

CUTLER, RL ;

DAVIES, AM ;

CREIGHTON, S ;

WARSHEL, A ;

MOORE, GR ;

SMITH, M ;

MAUK, AG .

BIOCHEMISTRY, 1989, 28 (08) :3188-3197

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