Carboxylate Shifts in the Active Site of the Hydroxylase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)
作者： Amy C. Rosenzweig , Christin A. Frederick , Stephen J. Lippard
DOI: 10.1007/978-94-009-0213-8_20
关键词:
摘要: Carboxylate anions constitute an especially versatile group of ligands in inorganic chemistry. Numerous complexes which the electron lone pairs a carboxylate anion are coordinated to one or more metal ions have been reported (R. C. Mehrotra, R. Bohra, 1983).
springer.com
sci-hub.st 参考文章(28)
S. J. Lippard, W. B. Tolman, R. Lynn Rardin, Monodentate carboxylate complexes and the carboxylate shift : implications for polymetalloprotein structure and function New Journal of Chemistry. ,vol. 15, pp. 417- 430 ,(1991)
S.K. Lee, J.C. Nesheim, J.D. Lipscomb, Transient intermediates of the methane monooxygenase catalytic cycle. Journal of Biological Chemistry. ,vol. 268, pp. 21569- 21577 ,(1993) , 10.1016/S0021-9258(20)80579-1
Ping Chen, Ursula Schulze-Gahmen, Enrico A. Stura, James Inglese, Dana L. Johnson, Ariane Marolewski, Stephen J. Benkovic, Ian A. Wilson, Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy. Journal of Molecular Biology. ,vol. 227, pp. 283- 292 ,(1992) , 10.1016/0022-2836(92)90698-J
K.E. Liu, S.J. Lippard, Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath). Effects of protein B, reductase, and substrate. Journal of Biological Chemistry. ,vol. 266, pp. 12836- 12839 ,(1991) , 10.1016/S0021-9258(18)98768-5
M P Hendrich, B G Fox, K K Andersson, P G Debrunner, J D Lipscomb, Ligation of the diiron site of the hydroxylase component of methane monooxygenase. An electron nuclear double resonance study Journal of Biological Chemistry. ,vol. 267, pp. 261- 269 ,(1992) , 10.1016/S0021-9258(18)48488-8
B G Fox, Y Liu, J E Dege, J D Lipscomb, Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. Journal of Biological Chemistry. ,vol. 266, pp. 540- 550 ,(1991) , 10.1016/S0021-9258(18)52470-4
J Green, H Dalton, Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity. Journal of Biological Chemistry. ,vol. 260, pp. 15795- 15801 ,(1985) , 10.1016/S0021-9258(17)36328-7
Amy C. Rosenzweig, Stephen J. Lippard, Determining the Structure of a Hydroxylase Enzyme That Catalyzes the Conversion of Methane to Methanol in Methanotrophic Bacteria Accounts of Chemical Research. ,vol. 27, pp. 229- 236 ,(1994) , 10.1021/AR00044A003
Amy C. Rosenzweig, Christin A. Frederick, Stephen J. Lippard, Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath) Journal of Molecular Biology. ,vol. 227, pp. 583- 585 ,(1992) , 10.1016/0022-2836(92)90913-5
Sang Kyu Lee, Brian G. Fox, Wayne A. Froland, John D. Lipscomb, Eckard Munck, A Transient Intermediate of the Methane Monooxygenase Catalytic Cycle Containing an FeIVFeIV Cluster Journal of the American Chemical Society. ,vol. 115, pp. 6450- 6451 ,(1993) , 10.1021/JA00067A086