Abstract
By using site-directed mutagenesis of the synthetic sperm whale myoglobin, the native distal histidine residue, at position 64 (the helical position E7), was substituted with a tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant was studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tyrosine.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
