Structural Studies of the Methylosinus trichosporium OB3b Soluble Methane Monooxygenase Hydroxylase and Regulatory Component Complex Reveal a Transient Substrate Tunnel.

Biochemistry
Jason C JonesJohn D Lipscomb

Abstract

The metalloenzyme soluble methane monooxygenase (sMMO) consists of hydroxylase (sMMOH), regulatory (MMOB), and reductase components. When sMMOH forms a complex with MMOB, the rate constants are greatly increased for the sequential access of O2, protons, and CH4 to an oxygen-bridged diferrous metal cluster located in the buried active site. Here, we report high-resolution X-ray crystal structures of the diferric and diferrous states of both sMMOH and the sMMOH:MMOB complex using the components from Methylosinus trichosporium OB3b. These structures are analyzed for O2 access routes enhanced when the complex forms. Previously reported, lower-resolution structures of the sMMOH:MMOB complex from the sMMO of Methylococcus capsulatus Bath revealed a series of cavities through sMMOH postulated to serve as the O2 conduit. This potential role is evaluated in greater detail using the current structures. Additionally, a search for other potential O2 conduits in the M. trichosporium OB3b sMMOH:MMOB complex revealed a narrow molecular tunnel, termed the W308-tunnel. This tunnel is sized appropriately for O2 and traverses the sMMOH-MMOB interface before accessing the active site. The kinetics of reaction of O2 with the diferrous sMMOH:MMOB co...Continue Reading

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Citations

Jan 26, 2021·Chemical Society Reviews·Christopher W Koo, Amy C Rosenzweig
Apr 23, 2021·Journal of the American Chemical Society·Christine E SchulzFrank Neese
Apr 23, 2021·Accounts of Chemical Research·Rahul Banerjee, John D Lipscomb
Jun 9, 2021·Biochemistry·Jason C JonesJohn D Lipscomb
Aug 28, 2021·International Journal of Environmental Research and Public Health·Xingchun LiYu Li
Aug 20, 2021·Frontiers in Bioengineering and Biotechnology·Kunal DuttaIbrahim Khalifa

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