Elucidating the coordination chemistry and mechanism of biological nitrogen fixation

被引：48

作者：

Dance, Ian ^{[1
]}

机构：

[1] Univ New S Wales, Sch Chem, Sydney, NSW 2052, Australia

来源：

CHEMISTRY-AN ASIAN JOURNAL | 2007年 / 2卷 / 08期

关键词：

allosterism; coordination chemistry; density functional calculations; nitrogen fixation; reaction mechanisms;

D O I：

10.1002/asia.200700131

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

How does the enzyme nitrogenase reduce the inert molecule N-2 to NH3 under ambient conditions that are so different from the energy-expensive conditions of the best industrial practices? This review focuses on recent theoretical investigations of the catalytic site, the iron-molybdenum cofactor FeMo-co, and the way in which it is hydrogenated by protons and electrons and then binds N-2. Density functional calculations provide reaction profiles and activation energies for possible mechanistic steps. This establishes a conceptual framework and the principles for the coordination chemistry of FeMo-co that are essential to the chemical mechanism of catalysis. The model advanced herein explains relevant experimental data.

引用

页码：936 / 946

页数：11

共 56 条

[1] Trapping a hydrazine reduction intermediate on the nitrogenase active site [J].

Barney, BM ;

Laryukhin, M ;

Igarashi, RY ;

Lee, HI ;

Dos Santos, PC ;

Yang, TC ;

Hoffman, BM ;

Dean, DR ;

Seefeldt, LC .

BIOCHEMISTRY, 2005, 44 (22) :8030-8037

[2] Intermediates trapped during nitrogenase reduction of N=N, CH3-N=NH, and H2N-NH2 [J].

Barney, BM ;

Yang, TC ;

Igarashi, RY ;

Dos Santos, PC ;

Laryukhin, M ;

Lee, HI ;

Hoffman, BM ;

Dean, DR ;

Seefeldt, LC .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (43) :14960-14961

[3] Breaking the N2 triple bond:: insights into the nitrogenase mechanism [J].

Barney, BM ;

Lee, HI ;

Dos Santos, PC ;

Hoffmann, BM ;

Dean, DR ;

Seefeldt, LC .

DALTON TRANSACTIONS, 2006, (19) :2277-2284

[4] Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis [J].

Barney, BM ;

Igarashi, RY ;

Dos Santos, PC ;

Dean, DR ;

Seefeldt, LC .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (51) :53621-53624

[5] A methyldiazene (HN=WN-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor:: Implications for mechanism [J].

Barney, Brett M. ;

Lukoyanov, Drnitriy ;

Yang, Tran-Chin ;

Dean, Dennis R. ;

Hoffman, Brian M. ;

Seefeldt, Lance C. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (46) :17113-17118

[6] Ab initio and experimental studies on the structure and relative stability of the cis-hydride-eta 2-dihydrogen complexes [{P(CH(2)CH(2)PPh(2))(3)}M(H)(eta(2)-H-2)](+) (M=Fe, Ru) [J].

Bianchini, C ;

Masi, D ;

Peruzzini, M ;

Casarin, M ;

Maccato, C ;

Rizzi, GA .

INORGANIC CHEMISTRY, 1997, 36 (06) :1061-1069

[7] Mechanism of molybdenum nitrogenase [J].

Burgess, BK ;

Lowe, DJ .

CHEMICAL REVIEWS, 1996, 96 (07) :2983-3011

[8] Enzymatic and catalytic reduction of dinitrogen to ammonia: Density functional theory characterization of alternative molybdenum active sites [J].

Cao, ZX ;

Zhou, ZH ;

Wan, HL ;

Zhang, QN .

INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY, 2005, 103 (03) :344-353

[9] Density functional study of the structure of the FeMo cofactor with an interstitial atom and homocitrate ligand ring opening [J].

Cao, ZX ;

Jin, X ;

Zhang, QN .

JOURNAL OF THEORETICAL & COMPUTATIONAL CHEMISTRY, 2005, 4 :593-602

[10] Isolation and characterization of an acetylene-resistant nitrogenase [J].

Christiansen, J ;

Cash, VL ;

Seefeldt, LC ;

Dean, DR .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (15) :11459-11464

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