Methane monooxygenase hydroxylase and B component interactions

Biochemistry
Jingyan ZhangJ D Lipscomb

Abstract

The interaction of the soluble methane monooxygenase regulatory component (MMOB) and the active site-bearing hydroxylase component (MMOH) is investigated using spin and fluorescent probes. MMOB from Methylosinus trichosporium OB3b is devoid of cysteine. Consequently, site-directed mutagenesis was used to incorporate single cysteine residues, allowing specific placement of the probe molecules. Sixteen MMOB Cys mutants were prepared and labeled with the EPR spin probe 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy (MSL). Spectral evaluation of probe mobility and accessibility to the hydrophilic spin-relaxing agent NiEDDA showed that both properties decrease dramatically for a subset of the spin labels as the complex with MMOH forms, thereby defining the likely interaction surface on MMOB. This surface contains MMOB residue T111 thought to play a role in substrate access into the MMOH active site. The surface also contains several hydrophilic residues and is ringed by charged residues. The surface of MMOB opposite the proposed binding surface is highly charged, consistent with solvent exposure. Probes of both of the disordered N- and C-terminal regions remain highly mobile and exposed to solvent in the MMOH complex. Spin-labelin...Continue Reading

References

Nov 7, 1996·Chemical Reviews·Bradley J. Wallar, John D. Lipscomb
Jul 5, 2005·Biophysical Journal·Christian AltenbachWayne L Hubbell

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Citations

Jun 15, 2007·Accounts of Chemical Research·E G KovalevaJ D Lipscomb
May 31, 2013·Biochemistry·Rahul BanerjeeJohn D Lipscomb
Mar 18, 2016·Microbiology and Molecular Biology Reviews : MMBR·Alan A DiSpiritoStéphane Vuilleumier
Jan 12, 2019·Annual Review of Biochemistry·Rahul BanerjeeJohn D Lipscomb
May 24, 2007·Accounts of Chemical Research·Leslie J Murray, Stephen J Lippard
Jun 9, 2021·Biochemistry·Jason C JonesJohn D Lipscomb

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