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Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenase
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UNSPECIFIED (1997) Purification and molecular characterization of the electron transfer protein of methanesulfonic acid monooxygenase. JOURNAL OF BACTERIOLOGY, 179 (6). pp. 1974-1979. ISSN 0021-9193.
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Abstract
A novel serine pathway methylotroph, strain M2, capable of utilizing methanesulfonic acid (MSA) as a sole source of carbon and energy was investigated, The initial step in the biodegradative pathway of MSA in strain M2 involved an inducible NADH-specific monooxygenase enzyme (MSAMO). Fractionation of MSAMO active cell extracts by ion-exchange chromatography led to the loss of MSAMO activity, Activity was restored by mixing three distinct protein fractions, designated A, B, and C. Further purification to homogeneity of component C indicated that the polypeptide was acidic, with a pI of 3.9, and contained an iron-sulfur center with spectral characteristics similar to those of other proteins containing Rieske [2Fe-2S] centers. The size of the protein subunit and the similarity of the N-terminal sequence to those of ferredoxin components of other oxygenase enzymes have suggested that component C is a specific electron transfer protein of the MSAMO which contains a Rieske [2Fe-2S] cluster, The gene encoding component C of MSAMO was cloned and sequenced, and the predicted protein sequence was compared with those of other Rieske [2Fe-2S]-center-containing ferredoxins, MSAMO appears to be a novel combination of oxygenase elements in which an enzyme related to aromatic-ring dioxygenases attacks a one-carbon (C-1) compound via monooxygenation.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QR Microbiology | ||||
Journal or Publication Title: | JOURNAL OF BACTERIOLOGY | ||||
Publisher: | AMER SOC MICROBIOLOGY | ||||
ISSN: | 0021-9193 | ||||
Official Date: | March 1997 | ||||
Dates: |
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Volume: | 179 | ||||
Number: | 6 | ||||
Number of Pages: | 6 | ||||
Page Range: | pp. 1974-1979 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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