Abstract:
:The functional role of residue Tyr-19 of Chromatium vinosum HiPIP has been evaluated by site-directed mutagenesis experiments. The stability of the [Fe4S4] cluster prosthetic center is sensitive to side-chain replacements. Polar residues result in significant instability, while nonpolar residues (especially with aromatic side chains) maintain cluster stability. Two-dimensional NMR data of native and mutant HiPIPs are consistent with a model where Tyr-19 serves to preserve the structural rigidity of the polypeptide backbone, thereby maintaining a hydrophobic barrier for exclusion of water from the cluster cavity. Solvent accessibility results in more facile oxidation of the cluster by atmospheric oxygen, with subsequent rapid hydrolysis of the [Fe4S4]3+ core.
journal_name
Proc Natl Acad Sci U S Aauthors
Agarwal A,Li D,Cowan JAdoi
10.1073/pnas.92.21.9440subject
Has Abstractpub_date
1995-10-10 00:00:00pages
9440-4issue
21eissn
0027-8424issn
1091-6490journal_volume
92pub_type
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