Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c'
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| 024 | 7 | 0 | |a 10.1007/s00775-015-1278-y |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-015-1278-y | ||
| 245 | 0 | 0 | |a Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c' |h [Elektronische Daten] |c [Dlzar Ghafoor, Demet Kekilli, Gaylany Abdullah, Florian Dworkowski, Hamid Hassan, Michael Wilson, Richard Strange, Michael Hough] |
| 520 | 3 | |a Cytochromes c', that occur in methanotrophic, denitrifying and photosynthetic bacteria, form unusual proximal penta-coordinate NO complexes via a hexa-coordinate distal NO intermediate. Their NO binding properties are similar to those of the eukaryotic NO sensor, soluble guanylate cyclase, for which they provide a valuable structural model. Previous studies suggested that hydrogen bonding between the displaced proximal histidine (His120) ligand (following its dissociation from heme due to trans effects from the distally bound NO) and a conserved aspartate residue (Asp121) could play a key role in allowing proximal NO binding to occur. We have characterized three variants of Alcaligenes xylosoxidans cytochrome c' (AXCP) where Asp121 has been replaced by Ala, Ile and Gln, respectively. In all variants, hydrogen bonding between residue 121 and His120 is abolished yet 5-coordinate proximal NO species are still formed. Our data therefore demonstrate that the His120-Asp121 bond is not essential for proximal NO binding although it likely provides an energy minimum for the displaced His ligand. All variants have altered proximal pocket structure relative to native AXCP. | |
| 540 | |a SBIC, 2015 | ||
| 690 | 7 | |a Cytochrome |2 nationallicence | |
| 690 | 7 | |a Nitric oxide |2 nationallicence | |
| 690 | 7 | |a X-ray crystallography |2 nationallicence | |
| 690 | 7 | |a Resonance Raman |2 nationallicence | |
| 690 | 7 | |a Spectroscopy |2 nationallicence | |
| 690 | 7 | |a Ligand binding |2 nationallicence | |
| 690 | 7 | |a CytCp : Cytochrome c' |2 nationallicence | |
| 690 | 7 | |a AXCP : Alcaligenes xylosoxidans cytochrome c' |2 nationallicence | |
| 690 | 7 | |a SFCP : Shewanella frigidimarina cytochrome c' |2 nationallicence | |
| 690 | 7 | |a SLS : Swiss Light Source |2 nationallicence | |
| 690 | 7 | |a 5c : 5-Coordinate |2 nationallicence | |
| 690 | 7 | |a 6c : 6-Coordinate |2 nationallicence | |
| 700 | 1 | |a Ghafoor |D Dlzar |u Faculty of Science and Education Science, University of Sulaimani, Sulaymaniyah, Iraq |4 aut | |
| 700 | 1 | |a Kekilli |D Demet |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | |
| 700 | 1 | |a Abdullah |D Gaylany |u Medical Research Center, Hawler Medical University, Erbil, Iraq |4 aut | |
| 700 | 1 | |a Dworkowski |D Florian |u Swiss Light Source, Paul Scherrer Institute (PSI), 5232, Villigen, Switzerland |4 aut | |
| 700 | 1 | |a Hassan |D Hamid |u College of Ibn-Alhaitham, University of Baghdad, Baghdad, Iraq |4 aut | |
| 700 | 1 | |a Wilson |D Michael |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | |
| 700 | 1 | |a Strange |D Richard |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | |
| 700 | 1 | |a Hough |D Michael |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/6(2015-09-01), 949-956 |x 0949-8257 |q 20:6<949 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-015-1278-y |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-015-1278-y |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Ghafoor |D Dlzar |u Faculty of Science and Education Science, University of Sulaimani, Sulaymaniyah, Iraq |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kekilli |D Demet |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Abdullah |D Gaylany |u Medical Research Center, Hawler Medical University, Erbil, Iraq |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Dworkowski |D Florian |u Swiss Light Source, Paul Scherrer Institute (PSI), 5232, Villigen, Switzerland |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hassan |D Hamid |u College of Ibn-Alhaitham, University of Baghdad, Baghdad, Iraq |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Wilson |D Michael |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Strange |D Richard |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hough |D Michael |u School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, Essex, UK |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/6(2015-09-01), 949-956 |x 0949-8257 |q 20:6<949 |1 2015 |2 20 |o 775 | ||