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Mechanism of T_1 relaxation in ^(13)CO complexed to an iron porphyrin: implications for CO bonding in heme proteins

Perkins, T. and Satterlee, J. D. and Richards, J. H. (1983) Mechanism of T_1 relaxation in ^(13)CO complexed to an iron porphyrin: implications for CO bonding in heme proteins. Journal of the American Chemical Society, 105 (5). pp. 1350-1354. ISSN 0002-7863. https://resolver.caltech.edu/CaltechAUTHORS:20150429-075633642

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Abstract

Chemical shifts and spin-lattice relaxation parameters for ^(13)CO bonded to the complex 1 -methylimidazole-iron protoporphyrin dimethyl ester are reported. The ^(13)CO chemical shifts are much different from those observed in the carbonyl vertebrate hemoglobins, but remarkably similar to that observed for the monomeric hemoglobin component from Glycera dibranchiata. The relaxation parameter, T_1, is shown to change dramatically upon ligation to both the hemin model system and to hemoglobin A. The mechanisms of spin-lattice relaxation are dominated by chemical shift anisotropy for ^(13)CO bound to both hemins and proteins, but, in the latter, dipole-dipole forces make an additional contribution to the overall relaxation rate.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/ja00343a047DOIArticle
http://pubs.acs.org/doi/abs/10.1021/ja00343a047PublisherArticle
Additional Information:© 1983 American Chemical Society. Received June 10, 1982. Contribution No. 6753 from the Departments of Chemistry, California Institute of Technology, Pasadena, California 91125, and the University of New Mexico. Albuquerque, New Mexico 87131. This work was supported by National Institutes of Health Grants GM 16424, HL 15162, and HL 13581. The HSX-360 Regional Facility (Stanford Magnetic Resonance Laboratory) was supported by National Institutes of Health Grant RR-00711 and National Science Foundation Grant GR-23633. J.D.S. also wishes to acknowledge support from Sandia Corp. during the preparation of this manuscript. Further, we gratefully acknowledge the cooperation of Professor J. D. Roberts and the use of his Bruker WH-180 spectrometer (supported by GM-11072). One of us (T.G.P.) thanks John G. Reynolds (S.M.R.L.) for help in obtaining the 8.45-T spectra and Dr. James Sudmeier (U.C. Riverside) for many helpful discussions.
Funders:
Funding AgencyGrant Number
NIHGM 16424
NIHHL 15162
NIHHL 13581
NIHRR-00711
NSFGR-23633
Sandia Corp.UNSPECIFIED
NIHGM-11072
Issue or Number:5
Record Number:CaltechAUTHORS:20150429-075633642
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150429-075633642
Official Citation:Mechanism of T1 relaxation in 13CO complexed to an iron porphyrin: implications for CO bonding in heme proteins T. Perkins, J. D. Satterlee, and J. H. Richards Journal of the American Chemical Society 1983 105 (5), 1350-1354 DOI: 10.1021/ja00343a047
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57076
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:01 May 2015 17:25
Last Modified:03 Oct 2019 08:20

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