Determining the Structure of a Hydroxylase Enzyme That Catalyzes the Conversion of Methane to Methanol in Methanotrophic Bacteria
作者： Amy C. Rosenzweig , Stephen J. Lippard
DOI: 10.1021/AR00044A003
关键词: Key features 、 Methanol 、 Enzyme 、 Protein subunit 、 Amino acid residue 、 Context (language use) 、 Bacteria 、 Biochemistry 、 Protein structure 、 Chemistry 、 Stereochemistry
摘要: The authors purpose in this Account is to review the structural work on hydroxylase carried out context of now known X-ray structure. address question, How well did noncrystallographic methods reveal key features protein structure? Of particular interest were following questions: (1) What structure holoenzyme, and how do three subunits interact: (2) many diiron centers are present, which subunit(s) accomodates(s) them? (3) exogeneous endogeneous species coordinated center, what specific amino acid residues serve as ligands? (4) does interact with other two MMO proteins? Discussion begins spectroscopic biochemical data obtained methodologies than crystallography resulting models pertaining each foregoing questions. then briefly discuss determination conclude by comparing derived from experiments. 60 refs., 6 figs.
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