Abstract
AbstractHemoglobin A and hemoglobin Kansas can exist in alternative forms in which the affinity of heme iron for NO is mediated either by pH or the presence of allosteric modifiers. In this study, we show that the superhyperfine (SHF) pattern observed in the EPR which arises from the heme iron‐NO complex can be correlated with a change in the affinity of the ligated tetrameric protein for NO. When a combination three‐line and nine‐line SHF pattern is observed, the nitrosyl hemoprotein is in a low affinity form while a nine‐line pattern alone is an expression of high affinity. A theory is presented relating SHF patterns to a molecular orbital picture of the nitrosyl heme complex. It is suggested that the change of SHF pattern correlated with an alteration of the affinity state of ligated hemoglobin is related to a structural change of the proximal imidazole ligand to the heme.
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.
