CaltechAUTHORS
Published January 18, 2010 | Version public
Journal Article Metadata-only

Determinants of Ligand Affinity and Heme Reactivity in H-NOX Domains

Creators

  • 1. ROR icon University of California, Berkeley
  • 2. ROR icon California Institute of Technology
  • 3. ROR icon Lawrence Berkeley National Laboratory

Abstract

O_2 balks at extra bulk: The introduction of distal-pocket bulk into the Thermoanaerobacter tengcongensis H-NOX (heme nitric oxide/oxygen) domain caused key changes in the protein structure. Rearrangement of the heme pocket resulted in dramatic differences in O_2-binding kinetics and heme reactivity (see picture).

Additional Information

© 2010 Wiley. Received: August 27, 2009; revised: October 28, 2009; Published online: December 16, 2009. Funding for this research was provided by the National Institutes of Health National Heart, Lung, and Blood Institute Award F32L090174 (E.E.W.), NIH grant GM 070671 (M.A.M.), and a grant from the Rogers Family Foundation (M.A.M.). We are grateful to Dr. Jay Winkler and the Beckman Institute Laser Resource Center at the California Institute of Technology for assistance with on-rate measurements, and members of the Marletta laboratory for critical reading of this manuscript. H-NOX=heme nitric oxide/oxygen.

Additional details

Identifiers

Eprint ID
17629
Resolver ID
CaltechAUTHORS:20100302-131334686

Funding

NIH
F32L090174
NIH
GM 070671
Rogers Family Foundation

Dates

Created
2010-03-08
Created from EPrint's datestamp field
Updated
2021-11-08
Created from EPrint's last_modified field