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1 M. capsulatus, along with other methanotrophs, has been
2 s P460 and cytochromes c' in N. europaea and M. capsulatus, confirm the importance of a heme-crosslin
5 , Em 7.0, was -250 mV for cytochrome c' from M. capsulatus Bath, which is well below the range of val
6 ence similarity of the P460 cytochromes from M. capsulatus Bath and N. europaea was low (24.3% of res
7 460 and used to identify a DNA fragment from M. capsulatus Bath that contains cyp, the gene encoding
8 53O was used to identify a DNA fragment from M. capsulatus Bath that contains occ, the gene encoding
9 f the diiron centers of the hydroxylase from M. capsulatus (Bath) at a modified gold electrode giving
11 tase complex (NADH dehydrogenase [NDH]) from M. capsulatus Bath, along with NADH and duroquinol, to e
12 with antibodies against cytochrome P460 from M. capsulatus Bath indicated that the expression level o
13 e findings extend previous work on pMMO from M. capsulatus (Bath) and provide new insight into the fu
14 methane monooxygenase effector protein from M. capsulatus (Bath) than that from M. trichosporium OB3
15 of soluble methane monooxygenase (sMMO) from M. capsulatus (Bath) have clarified discrepancies that e
16 that a cytochrome P460 similar to that from M. capsulatus Bath may be present in the type II methano
18 M. flagellatus were more similar to those in M. capsulatus and M. extorquens than to the ones in the
20 ereas a metal center occupied by zinc in the M. capsulatus (Bath) pMMO structure is occupied by coppe
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