Methane biochemistry

Castro CE, RS Wade, NO Belser (1985) Biodehalogenation reactions of cytochrome P-450 with polyhalo-methanes. Biochemistry 24 204-210. 

Fox BG, Bomeman JG, Wackett LP, et al. 1990. Haloalkane oxidation by the soluble methane monooxygenase irom Methylosinus trichosporium OB3b Mechanistic and environmental implications. Biochemistry 29 6419-6427. 

Lipscomb ID (1994) Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol 48 371-399. 

Polyesters, such as microbially produced poly[(P)-3-hydroxybutyric acid] [poly(3HB)], other poly[(P)-hydroxyalkanoic acids] [poly(HA)] and related biosynthetic or chemosynthetic polyesters are a class of polymers that have potential applications as thermoplastic elastomers. In contrast to poly(ethylene) and similar polymers with saturated, non-functionalized carbon backbones, poly(HA) can be biodegraded to water, methane, and/or carbon dioxide. This review provides an overview of the microbiology, biochemistry and molecular biology of poly(HA) biodegradation. In particular, the properties of extracellular and intracellular poly(HA) hydrolyzing enzymes [poly(HA) depolymerases] are described. 

Bloxham, D.P., and Cooper, C.K. (1982) Formation of a polymethylene bis(disulfide) inter-subunit crosslink between cys-281 residues in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase using octamethylene bzs-(methane[35]thiosulfonate). Biochemistry 21, 1807. 

Schiitz H, Seiler W, Comad R. 1990. Influence of soil temperatme on methane emission from rice paddy fields. Biochemistry 11 77-95. 

Yao H, Conrad R. 1999. Thermodynamics of methane production in different rice paddy soils from China, the Philippines and Italy. Soil Biology and Biochemistry 31 463-473. 

Paul FA, Qark FE (1989) Soil microbiology and biochemistry. Academic Press, New York Pecher K, HaderUne SB, Schwarzenbach RP (2002) Reduction of polyhalogenated methanes by surface— b Fe(ll) in aqueous suspensions of iron oxides. Environ Sci Technol 36 1734-1741 Penrose WR, Metta DN, Hyfko JM, Rinkel LA (1987) The reduction of plutonium (V) by aquatic sediments. J Environ Radioact 5 169-184... 

The sodium acetate-acetic acid combination is one of the most widely used buffers, and is usually referred to simply as acetate buffer. Other buffer combinations commonly employed in chemistry and biochemistry include carbonate-bicarbonate (sodium carbonate-sodium hydrogen carbonate), citrate (citric acid-trisodium citrate), phosphate (sodium dihydrogen phosphate-disodium hydrogen phosphate), and tris [tris(hydroxymethyl)amino-methane-HCl]. 

Wallar, B. J. Lipscomb, J. D. Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry 2001, 40(7), 2220-2233. 

Lieberman, R. L. Rosenzweig, A. C. Biological methane oxidation regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 2004, 39(3), 147-164. 

Kitmitto, A. Myronova, N. Basu, R Dalton, H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 2005, 44(33), 10954-10965. 

Chang, S-L., Wallar, B.J., Lipscomb, J.D., and Mayo, K.H. (2001) Residues in Methylosinus trichosporium OB3b methane monooxygenase component B involved in molecular interactions with reduced- and oxidized-hydroxylase component A role for the N-terminus, Biochemistry 40, 9539-9551. 

Gassner, G.T., Lippard, S.J. (1999) Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38, 12768-12785. 

Muller, J., Lugovskoy, A. A., Wagner, G., and Lippard, S.J. (2002) NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase. Biochemistry 41, 42-51. 

Ruzicka, F., Huang, D-S., Donnelly, M L, and Frey P.A. (1990) Methane monooxygenase catalyzed oxygenation of of 1, 1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates, Biochemistry 29, 1696-1700. s... 

Davydov, R., Valentine, A. M., Komar-Panicucci, S., Hoffman, B. M., and Lippard, S. J., 1999, An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77K the effects of component interactions and the binding of small molecules to the diiron(lll) center. Biochemistry 38 418864197. 

Fox, B. G., Bomeman, J. G., Wackett, L. P., and Lipscomb, J. D., 1990, Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b mechanistic and environmental implications. Biochemistry 29 6419fi6427. 

Gallagher, S. C., Callaghan, A. J., Zhao, J., Dalton, H., and Trewhella, J., 1999, Global Conformational Changes Control the Reactivity of Methane Monooxygenase, Biochemistry 38 6572fi6760. 

Lee, S. K., and Lipscomb, J. D., 1999, Oxygen activation catalyzed by methane monooxygenase hydroxylase component proton delivery during the 060 bond cleavage steps. Biochemistry 38 4423n4432. 

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