Abstract：
:A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is presented. (15)N relaxation measurements confirm earlier results indicating that R. capsulatus ferrocytochrome c(2) exhibits minor rotational anisotropy in solution. The current study is focused on the use of deuterium relaxation in side chain methyl groups, which has been shown to provide a detailed and accurate measure of internal dynamics. Results obtained indicate that the side chains of ferrocytochrome c(2) exhibit a wide range of motional amplitudes, but are more rigid than generally found in the interior of nonprosthetic group bearing globular proteins. This unusual rigidity is ascribed to the interactions of the protein with the large heme prosthetic group. This observation has significant implications for the potential of the heme-protein interface to modulate the redox properties of the protein and also points to the need for great precision in the design and engineering of heme proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Flynn PF,Bieber Urbauer RJ,Zhang H,Lee AL,Wand AJdoi
10.1021/bi0102252subject
Has Abstractpub_date
2001-06-05 00:00:00pages
6559-69issue
22eissn
0006-2960issn
1520-4995pii
bi0102252journal_volume
40pub_type
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