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Role of Hydrogenase

Bryant RD, Laishley EJ. 1990. The role of hydrogenase in anaerobic biocorrosion. Can J Microbiol 36 259-64. [Pg.259]

Church DL, Rabin HR, Laishley EJ. 1988. Role of hydrogenase 1 of Clostridium pasteurianium in the reduction of metronidazole. Biochem Pharmacol 37 1525-34. [Pg.260]

In addition to these, it should also be noted that this model is also a bacteria-speciflc model and thus cannot explain all various types of MIC. Also, the model s main factor is hydrogenase-positive SRB, and therefore, the possible role of hydrogenase-negative SRB in enhancing corrosion (such as hydrogenase-negative Desulfococcus multivorans ) is overlooked. [Pg.106]

Name referred to in literature and references Main mechanisms Role of hydrogenase... [Pg.1286]

Name Referred to in the Literature and References Main Mechanisms Role of Hydrogenase... [Pg.754]

S. Da SUva, R. Basseguy, and A. Bergel, The role of hydrogenases in the anaerobic microbiologi-cally influenced corrosion of steels. Bioelectrochemistry 56 77 (2002). [Pg.773]

The biologically uncommon Ni center associated with FeS clusters is a powerful and unique catalytic unity. In this chapter we have reviewed the structural and mechanistic aspects of three NiFeS centers the active site of hydrogenase and Clusters A and C of CODH/ACS. In the former, the association of a Ni center with the most unusual FeCOCN2 unit is a fascinating one. Model chemists, spectroscopists, and crystallographers have joined efforts to try and elucidate the reaction mechanism. Although a consensus is being slowly reached, the exact roles of the different active site components have not yet been fully established. Ni appears to be the catalytic center proper, whereas the unusual Fe center may be specially suited to bind a by-... [Pg.326]

In addition, the [NiFe] hydrogenase from D. fructosovorans is very similar to D. gigas hydrogenase, and its structure has been solved 185). In order to understand the role of the [3Fe-4S] cluster, a Pro-432Cys mutant was produced. In this mutant the conversion of a [3Fe-4S] into a [4Fe-4S] center was proven by EPR and X-ray crystallography. [Pg.393]

Midpoint potential values are useful quantitites for defining the role of the various centers in the system. In some instances, these values have even been used to predict the location of the centers in the electron transfer chain, assuming that the potential increases along the chain from the electron donor to the electron acceptor. In several oxidoreductases, however, the measured potential of some centers was found to be clearly outside the range defined by the donor and the acceptor, which raised an intriguing question as to their function. This was observed, for instance, in the case of the [4Fe-4S] (Eni = -320 mV) center in E. coli fumarate reductase (249), the [3Fe-4S] + (Era = -30 mV) center in D. gigas hydrogenase (207), and the low-potential [4Fe-4S] + + (E, = 200 and -400 mV) centers in E. [Pg.475]

Ma K, R Weiss, MWW Adams (2000) Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J Bacteriol 182 1864-1871. [Pg.190]

Aich P, Sen R, Dasgupta D (1992b) Role of magnesium ion in the interaction between chromomycin A3 and DNA binding of chromomycin A3 — Mg + complexes with DNA. Biochemistry 31 2988-2997 Akman SA, Doroshow JJH, Thomas G, Burke J, Dizdaroglus M (1992) DNA base modifications induced in isolated human chromatin by NADH de hydrogenase-catalyzed reduction of doxorubicin. Biochemistry, 31 3500-3506... [Pg.181]

S.3. The role of the C-terminal cleavage of the large subunits of the NiFe(Se) hydrogenases... [Pg.87]


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Hydrogenase

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