Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c `

S.G. Kruglik , J.C. Lambry , S. Cianetti , J.L. Martin , R.R. Eady , C.R. Andrew , M. Negrerie

Bibtex , URL
Journal of Biological Chemistry, 282, 7, 5053-5062
Published 16 Feb. 2007
DOI: 10.1074/jbc.M604327200
ISSN: 0021-9258


The bacterial heme protein cytochrome c' from Alcaligenes xylosoxidans (AXCP) reacts with nitric oxide (NO) to form a 5-coordinate ferrous nitrosyl heme complex. The crystal structure of ferrous nitrosyl AXCP has previously revealed that NO is bound in an unprecedented manner on the proximal side of the heme. To understand how the protein structure of AXCP controls NO dynamics, we performed absorption and Raman time-resolved studies at the heme level as well as a molecular computational dynamics study at the entire protein structure level. We found that after NO dissociation from the heme iron, the structure of the proximal heme pocket of AXCP confines NO close to the iron so that an ultrafast (7 ps) and complete (99 +/- 1\%) geminate rebinding occurs, whereas the proximal histidine does not rebind to the heme iron on the timescale of NO geminate rebinding. The distal side controls the initial NO binding, whereas the proximal heme pocket controls its release. These dynamic properties allow the trapping of NO within the protein core and represent an extreme behavior observed among heme proteins.