ALDEHYDE OXIDOREDUCTASE ACTIVITY IN DESULFOVIBRIO-GIGAS - IN-VITRO RECONSTITUTION OF AN ELECTRON-TRANSFER CHAIN FROM ALDEHYDES TO THE PRODUCTION OF MOLECULAR-HYDROGEN

被引:54
作者
BARATA, BAS
LEGALL, J
MOURA, JJG
机构
[1] UNIV GEORGIA, DEPT BIOCHEM, ATHENS, GA 30602 USA
[2] UNIV LISBON, FAC CIENCIAS, DEPT QUIM, LISBON, PORTUGAL
[3] UNIV NOVA LISBOA, FAC CIENCIAS & TECNOL, DEPT QUIM, P-2825 MONTE DE CAPARICA, PORTUGAL
关键词
D O I
10.1021/bi00094a012
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
The molybdenum[iron-sulfur] protein, first isolated from Desulfovibrio gigas by Moura et al. [Moura, J. J. G., Xavier, A. V., Bruschi, M., LeGall, J., Hall, D. O., & Cammack, R. (1976) Biochem. Biophys. Res. Commun. 72, 782-789], was later shown to mediate the electronic flow from salicylaldehyde to a suitable electron acceptor, 2,6-dichlorophenolindophenol (DCPIP) [Turner, N., Barata, B., Bray, R. C., Deistung, J., LeGall J., & Moura, J. J. G. (1987) Biochem. J. 243,755-761]. The DCPIP-dependent aldehyde oxidoreductase activity was studied in detail using a wide range of aldehydes and analogues. Steady-state kinetic analysis (K(M) and V(max)) was performed for acetaldehyde, propionaldehyde, benzaldehyde, and salicylaldehyde in excess DCPIP concentration, and a simple Michaelis-Menten model was shown to be applicable as a first kinetic approach. Xanthine, purine, allopurinol, and N1-methylnicotinamide (NMN) could not be utilized as enzyme substrates. DCPIP and ferricyanide were shown to be capable of cycling the electronic flow, whereas other cation and anion dyes [O2 and NAD(P)+] were not active in this process. The enzyme showed an optimal pH activity profile around 7.8. This molybdenum hydroxylase was shown to be part of an electron-transfer chain comprising four different soluble proteins from D. gigas, with a total of 11 discrete redox centers, which is capable of linking the oxidation of aldehydes to the reduction of protons.
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页码:11559 / 11568
页数:10
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