Allosteric control of internal electron transfer in cytochrome cd1 nitrite reductase

被引：40

作者：

Farver, O ^{[1
]}

Kroneck, PMH

Zumft, WG

Pecht, I

机构：

[1] Danish Univ Pharmaceut Sci, Dept Analyt Chem, DK-2100 Copenhagen, Denmark

[2] Univ Konstanz, Fachbereich Biol, D-78457 Constance, Germany

[3] Univ Karlsruhe, Lehrstuhl Mikrobiol, D-76128 Karlsruhe, Germany

[4] Weizmann Inst Sci, Dept Immunol, IL-76100 Rehovot, Israel

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 13期

关键词：

D O I：

10.1073/pnas.0932693100

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Cytochrome cd(1) nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in the Pseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between the c and the d(1) hemes. The interactions are expressed both in dramatic changes in the internal electron-transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intraprotein control of the electron-transfer rates by allosteric interactions.

引用

页码：7622 / 7625

页数：4

共 15 条

[1] Dissimilatory nitrite and nitric oxide reductases [J].

Averill, BA .

CHEMICAL REVIEWS, 1996, 96 (07) :2951-2964

[2] ALLOSTERIC COOPERATIVE INTERACTIONS AMONG REDOX SITES OF PSEUDOMONAS CYTOCHROME-OXIDASE [J].

BLATT, Y ;

PECHT, I .

BIOCHEMISTRY, 1979, 18 (13) :2917-2922

[3] Domain swing upon his to ala mutation in nitrite reductase of Pseudomonas aeruginosa [J].

Brown, K ;

Roig-Zamboni, V ;

Cutruzzola, F ;

Arese, M ;

Sun, WL ;

Brunori, M ;

Cambillau, C ;

Tegoni, M .

JOURNAL OF MOLECULAR BIOLOGY, 2001, 312 (03) :541-554

[4] Two enzymes with a common function but different heme ligands in the forms as isolated.: Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha [J].

Cheesman, MR ;

Ferguson, SJ ;

Moir, JWB ;

Richardson, DJ ;

Zumft, WG ;

Thomson, AJ .

BIOCHEMISTRY, 1997, 36 (51) :16267-16276

[5] The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase [J].

Farver, O ;

Eady, RR ;

Abraham, ZHL ;

Pecht, I .

FEBS LETTERS, 1998, 436 (02) :239-242

[6] Intramolecular electron transfer in cytochrome cd1 nitrite reductase from Pseudomonas stutzeri;: kinetics and thermodynamics [J].

Farver, O ;

Kroneck, PMH ;

Zumft, WG ;

Pecht, I .

BIOPHYSICAL CHEMISTRY, 2002, 98 (1-2) :27-34

[7] THE ANATOMY OF A BIFUNCTIONAL ENZYME - STRUCTURAL BASIS FOR REDUCTION OF OXYGEN TO WATER AND SYNTHESIS OF NITRIC-OXIDE BY CYTOCHROME CD(1) [J].

FULOP, V ;

MOIR, JWB ;

FERGUSON, SJ ;

HAJDU, J .

CELL, 1995, 81 (03) :369-377

[8] Electron transfer in proteins [J].

Gray, HB ;

Winkler, JR .

ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :537-561

[9] Cytochrome cd1 from Parococcus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior [J].

Koppenhöfer, A ;

Turner, KL ;

Allen, JWA ;

Chapman, SK ;

Ferguson, SJ .

BIOCHEMISTRY, 2000, 39 (15) :4243-4249

[10] Cytochrome C oxidase: Structure and spectroscopy [J].

Michel, H ;

Behr, J ;

Harrenga, A ;

Kannt, A .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1998, 27 :329-356

← 1 2 →