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Active-site cobalt(II)-substituted horse liver alcohol dehydrogenase: characterization of intermediates in the oxidation and reduction processes as a function of pH.
Sartorius C, Gerber M, Zeppezauer M, Dunn MF. Sartorius C, et al. Among authors: zeppezauer m. Biochemistry. 1987 Feb 10;26(3):871-82. doi: 10.1021/bi00377a031. Biochemistry. 1987. PMID: 3567150
C., MacGibbon, A. K. H., Dietrich, H., Zeppezauer, M., & Dunn, M. F. (1983) Biochemistry 22, 3424-3431]. In this study, UV-visible spectroscopy and rapid-scanning stopped-flow (RSSF) kinetic methods are used to detect and identify intermediates in the LAD …
C., MacGibbon, A. K. H., Dietrich, H., Zeppezauer, M., & Dunn, M. F. (1983) Biochemistry 22, 3424-3431]. In this st …
Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotide.
Dietrich H, Maret W, Wallén L, Zeppezauer M. Dietrich H, et al. Among authors: zeppezauer m. Eur J Biochem. 1979 Oct;100(1):267-70. doi: 10.1111/j.1432-1033.1979.tb02057.x. Eur J Biochem. 1979. PMID: 226360 Free article. No abstract available.
86 results