Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 32, Pages 13071-13076Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1101459108
Keywords
direct electrochemistry; NMR spectroscopy; X-ray crystallography
Categories
Funding
- Uehara Memorial Foundation
- Canada Research Chair
- Canadian Blood Services-Canadian Institutes of Health Research
- CIHR [MOP-49597]
- Canadian Foundation for Innovation
- USDE, Office of Biological and Environmental Research
- National Institutes of Health, National Center for Research Resources
- National Institute of General Medical Sciences
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IsdI, a heme-degrading protein from Staphylococcus aureus, binds heme in a manner that distorts the normally planar heme prosthetic group to an extent greater than that observed so far for any other heme-binding protein. To understand better the relationship between this distinct structural characteristic and the functional properties of IsdI, spectroscopic, electrochemical, and crystallo-graphic results are reported that provide evidence that this heme ruffling is essential to the catalytic activity of the protein and eliminates the need for the water cluster in the distal heme pocket that is essential for the activity of classical heme oxygenases. The lack of heme orientational disorder in 1H-NMR spectra of the protein argues that the catalytic formation of beta- and delta-biliverdin in nearly equal yield results from the ability of the protein to attack opposite sides of the heme ring rather than from binding of the heme substrate in two alternative orientations.
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