article · 16/02/2007
Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c `
Résumé
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.
Citer cet article
Kruglik, S.-G., Lambry, J.-C., Cianetti, S., Martin, J.-L., Eady, R.-R., Andrew, C.-R., & Negrerie, M. (2007). Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c `. Journal of Biological Chemistry, 282(7), 5053-5062. https://doi.org/10.1074/jbc.M604327200@article{Kruglik2007_68,
author = {Kruglik, Sergei G. and Lambry, Jean-Christophe and Cianetti, Simona and Martin, Jean-Louis and Eady, Robert R. and Andrew, Colin R. and Negrerie, Michel},
year = {2007},
month = {2},
title = {Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c `},
journal = {Journal of Biological Chemistry},
publisher = {AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC},
volume = {282},
number = {7},
pages = {5053-5062},
address = {9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA},
abstract = {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\textbackslash{}\%) 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.},
url = {http://www.dx.doi.org/10.1074/jbc.M604327200},
doi = {10.1074/jbc.M604327200},
issn = {0021-9258},
}TY - JOUR
AU - Kruglik, Sergei G.
AU - Lambry, Jean-Christophe
AU - Cianetti, Simona
AU - Martin, Jean-Louis
AU - Eady, Robert R.
AU - Andrew, Colin R.
AU - Negrerie, Michel
PY - 2007
DA - 2007/02/16
TI - Molecular basis for nitric oxide dynamics and affinity with Alcaligenes xylosoxidans cytochrome c `
JO - Journal of Biological Chemistry
VL - 282
IS - 7
PB - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
SN - 0021-9258
AB - 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.
SP - 5053
EP - 5062
DO - 10.1074/jbc.M604327200
UR - http://www.dx.doi.org/10.1074/jbc.M604327200
ER -