Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification.

@article{Lloyd1997InactivationOT,
  title={Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification.},
  author={John S. Lloyd and Avninder S Bhambra and John Colin Murrell and Howard Dalton},
  journal={European journal of biochemistry},
  year={1997},
  volume={248 1},
  pages={
          72-9
        }
}
The regulatory protein B of soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), exists as a mixture of the full-length active form and truncated forms, B' and B". Electrospray ionisation mass spectrometry (ESI-MS) was used to identify a cleavage site between Met12 and Gly13, such that 12 amino acids were lost from the N-terminus of protein B. This truncate was designated B' and molecular masses were assigned to proteins B and B' of 15,852.6+/-0.4 Da and 14,629.5+/-0.3 Da… 

Structure of the soluble methane monooxygenase regulatory protein B.

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Improved System for Protein Engineering of the Hydroxylase Component of Soluble Methane Monooxygenase

Substantial development of the method to produce a system for the facile construction and expression of mutants of the hydroxylase component of sMMO is reported, demonstrating proof of the principle for protein engineering of this uniquely versatile enzyme.

Molecular genetics and microbiology of bioremediation using methane-oxidising bacteria

Results from site-directed mutagenesis created four new mutants in addition to performing further characterization of another two, and indicated that radical chemistry at this position is not essential for monooxygenase activity toward a number of aliphatic and aromatic hydrocarbons.

Molecular biology and regulation of methane monooxygenase

A model for copper regulation based on results from Northern analysis, primer-extensions and new sequence data is presented, and a number of unanswered questions for future studies are raised.

Homologous expression of soluble methane monooxygenase genes in Methylosinus trichosporium OB3b.

This is the first report of homologous sMMO expression in a methanotroph with enzyme activities that are comparable to the activity reported in wild-type strains.

X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase.

X-ray structures of native and SeMet forms of the PH hydroxylase (PHH) in complex with its regulatory protein (PHM) are determined, suggesting that the regulatory component may function to block undesired reduction of oxygenated intermediates during the catalytic cycle.

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