Acetylene as a suicide substrate and active site probe for methane monooxygenase from <i>Methylococcus capsulatus</i> (Bath) Export

@article{citeulike:4953052, abstract = {Acetylene was shown to be an inhibitor of cell-free methane monooxygenase (MMO) activity in Methylococcus capsulatus (Bath). Inhibition was demonstrated for both the soluble and particulate forms of the enzyme and was dependent on the presence of both NADH and oxygen. Inactivation of the enzyme complex was irreversible and was due to binding of the acetylene to specific proteins of the enzyme complex. The use of radiolabelled [14C]acetylene provided a method for visualisation of the bound inhibitor: protein complex on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). Acetylene was shown to bind to proteins which are associated with methane-oxidising activity and it is proposed that acetylene acts as a suicide substrate.}, address = {Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, U.K.}, author = {Prior, S. D. and Dalton, H.}, citeulike-article-id = {4953052}, citeulike-linkout-0 = {http://dx.doi.org/10.1111/j.1574-6968.1985.tb00843.x}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/119518082/ABSTRACT}, doi = {10.1111/j.1574-6968.1985.tb00843.x}, journal = {FEMS Microbiology Letters}, keywords = {actelyene, c2h2, ch4, inhibition, methane, methane-oxidation, methanotrophic}, number = {1-2}, pages = {105--109}, posted-at = {2009-06-25 10:40:59}, priority = {4}, title = {Acetylene as a suicide substrate and active site probe for methane monooxygenase from <i>Methylococcus capsulatus</i> (Bath)}, url = {http://dx.doi.org/10.1111/j.1574-6968.1985.tb00843.x}, volume = {29}, year = {1985} }

TY - JOUR ID - citeulike:4953052 L3 - citeulike-article-id:4953052 N2 - Acetylene was shown to be an inhibitor of cell-free methane monooxygenase (MMO) activity in Methylococcus capsulatus (Bath). Inhibition was demonstrated for both the soluble and particulate forms of the enzyme and was dependent on the presence of both NADH and oxygen. Inactivation of the enzyme complex was irreversible and was due to binding of the acetylene to specific proteins of the enzyme complex. The use of radiolabelled [14C]acetylene provided a method for visualisation of the bound inhibitor: protein complex on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). Acetylene was shown to bind to proteins which are associated with methane-oxidising activity and it is proposed that acetylene acts as a suicide substrate. IS - 1-2 JF - FEMS Microbiology Letters AD - Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, U.K. EP - 109 TI - Acetylene as a suicide substrate and active site probe for methane monooxygenase from <i>Methylococcus capsulatus</i> (Bath) VL - 29 SP - 105 KW - actelyene KW - c2h2 KW - ch4 KW - inhibition KW - methane KW - methane-oxidation KW - methanotrophic AU - Prior, SD AU - Dalton, H PY - 1985/// UR - http://dx.doi.org/10.1111/j.1574-6968.1985.tb00843.x ER -