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Spectroscopic studies dehydrogenase

Labesse, G., Ferrari, D., Chen, Z-W., Rossi, G-L., Kuusk, V., Mclntire, W. S., Mathews, F. S., 1998, Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AMI, /. Biol. Chem. 273 25703925712. [Pg.142]

Staples, C. R., Heo, J., Spangler, N. J., Kerby, R. L., Roberts, G. P., and Ludden, P. W., 1999, Rhodospirillum rubrum CO dehydrogenase. Part 1. Spectroscopic studies of CODH variant C531A indicate the presence of a binuclear [FeNi] Cluster, J. Am. Chem. Soc. in press. [Pg.517]

Deng, H., Zheng, J., Burgner, J., and Callender, R., Molecular properties of pyruvate bound to lactate dehydrogenase A Raman spectroscopic study, Proc. Nat. Acad. Sci., USA 86, 4484-4488 (1989). [Pg.361]

K. W., Sloan, D., VanderSteen, R., Yue, K. T. (1988) The Molecular Properties of p-Dimethylamino Benzaldehyde Bound to Liver Alchohol Dehydrogenase a Raman Spectroscopic Study Biochemistry 27, 3672-3681. [Pg.1413]

R. (1991) Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques, Biochemistry 30, 8804-8811. [Pg.1414]

R. (1992) Raman Spectroscopic Studies of the Effects of Substrate Binding on Coenzymes Bound to Lactate Dehydrogenase, J. Am. Chem. Soc. 114, 7997-8003. [Pg.1414]

Zhang B, Hemann CF, Hille R (2010) Kinetic and spectroscopic studies of the [molybdenum-copper] CO dehydrogenase from Oligotropha carboxidovorans. J Biol Chem 285 12571-12578. doi 10.1074/jbc.M109.076851... [Pg.264]

Much interest has been placed on understanding the enzymatic reaction pathways so that they can be reproduced in vitro. In particular, CO dehydrogenase has been studied in detail and the cycle of production of acetic acid from CO2 [126] is quite well understood (Scheme 1.19). The active site contains a S4pe4-Ni cluster. The role of the different metal centers in the process has been a matter of discussion. Through spectroscopic studies on the enzyme, using Fe-labeled species, the Fe atom (Scheme 1.19 a [127]) was suggested to be involved in the... [Pg.29]

Oxidation by direct H transfer from the a-carbon of alcohols to the pyrroloquinoline quinone (PQQ) cofactor of alcohol dehydrogenases was studied using ab initio quantum mechanical methods <2001JCC1732>. Energies and geometries were calculated at the 6-31G(d,p) level of theory, results were compared to available structural and spectroscopic data, and the role of calcium in the enzymatic reaction was explored. Transition state searches at the semi-empirical and STO-3G(d) level of theory provided evidence that direct transfer from the alcohol to C-5 of PQQ is energetically feasible. [Pg.1202]

For example, liver alcohol dehydrogenase was crystallized as the enzyme N AD1 p-bromobenzyl alcohol complex with saturating concentrations of substrates in an equilibrium mixture51b and studied at low resolution. Transient kinetic studies or direct spectroscopic determinations led to the conclusion that the internal equilibrium (E NAD alcohol = E NADH aldehyde) favors the NAD1 alcohol complex.52 Subsequently, the complex was studied at higher resolution, and the basic structural features were confirmed with a... [Pg.773]

In 1915, Harden and Norris observed that dried yeast, when mixed with lactic acid, reduced methylene blue and formed pyruvic acid 4). Thirteen years later Bernheim prepared an extract from acetone-dried baker s yeast, which had lactate dehydrogenase activity (5). Bach and co-workers demonstrated that the lactate dehydrogenase activity was associated with a 6-type cytochrome, which they named cytochrome 62 (6). In 1954, the enzyme was crystallized, enabling the preparation of pure material and the identification of flavin mononucleotide as a second prosthetic group (2). Since then, significant advances have been made in the analysis of the structure and function of the enzyme. Much of the earlier work on flavocytochrome 62 has already been summarized in previous review articles (7-10). In this article we shall describe recent developments in the study of this enzyme, ranging fi om kinetic, spectroscopic, and structural data to the impact of recombinant DNA technology. [Pg.259]


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See also in sourсe #XX -- [ Pg.42 , Pg.43 , Pg.44 ]




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