ISSN:
1432-1017
Keywords:
Myoglobin
;
XANES
;
synchrotron radiation
;
protein structure
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract The ligand bonding geometry of carboxy-and cyanomet-myoglobin (MbCO and MbCN) has been measured by the XANES method (X-ray Absorption Near Edge Structure). A comparison between the ligand bonding geometry of carboxy- and cyanomet-myoglobin and of chelated protoheme methyl ester shows that the bent Fe−C−O configuration is the same in both systems. Therefore, we suggest that this configuration is not associated with any steric contraint imposed by the side chains of the aminoacid residues at the distal side of the heme pocket.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00260397
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