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Carbonyl Sulfide Inhibition of CO Dehydrogenase from Rhodospirillum rubrum Public Deposited

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  • Carbonyl sulfide (COS) has been investigated as a rapid-equilibrium inhibitor of CO oxidation by the CO dehydrogenase purified from Rhodospirillum rubrum. The kinetic evidence suggests that the inhibition by COS is largely competitive versus CO (Ki = 2.3 pM) and uncompetitive versus methylviologen as electron acceptor (Ki = 15.8 pM). The data are compatible with a ping-pong mechanism for CO oxidation and COS inhibition. Unlike the substrate CO, COS does not reduce the iron-sulfur centers of dye-oxidized CO dehydrogenase and thus is not an alternative substrate for the enzyme. However, like CO, COS is capable of protecting CO dehydrogenase from slow-binding inhibition by cyanide. A true binding constant (KD) of 2.2 pM for COS has been derived on the basis of the saturable nature of COS protection against cyanide inhibition. The ability of CO, C02, COS, and related CO/CO, analogues to reverse cyanide inhibition of CO dehydrogenase is also demonstrated. The kinetic results are interpreted in terms of two binding sites for CO on CO dehydrogenase from R. rubrum.
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  • Hyman, M. R., Ensign, S. A., Arp, D. J., & Ludden, P. W. (1989). Carbonyl Sulfide Inhibition of CO Dehydrogenase from Rhodospirillum rubrum. Biochemistry, 28(17), 6821-6826. doi:10.1021/bi00443a007
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  • This research was supported by the College of Agricultural and Life Sciences at the University of Wisconsin-Madison and by Grant DEFG02- 87ER13691 to P.W.L. from the US. Department of Energy. S.A.E. was supported by Training Grant GM07215 from the National Institutes of Health, and M.R.H. was supported by Grant DE-FG03- 84ER13257 to D.J.A. from the US. Department of Energy during this study.
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  • description.provenance : Made available in DSpace on 2011-08-08T16:35:37Z (GMT). No. of bitstreams: 1 ArpDanielJ.Botany.Carbonylsulfideinhibition.pdf: 766628 bytes, checksum: 79c2c6a10e0387adb80c879be6b8c361 (MD5) Previous issue date: 1989
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