Journal article
Spectroscopic and kinetic aspects of Elephas maximus hemoglobin
European journal of biochemistry, v 189(1), pp 185-191
Apr 1990
PMID: 2158890
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Abstract
In comparison with myoglobin and human and Glycera dibranchiata hemoglobins, the heme distal side amino acid exchanges within the heme environment of elephant tetrameric hemoglobin (Hbe) only slightly affect the electronic and ESR spectra of Hbe(III) and Hbe(II) derivatives, several of which were prepared and characterized by optical and ESR spectroscopy. Addition of 2,3‐bisphosphoglycerate [Gri(2,3)P2] or inositol hexakisphosphate to Hbe(II)NO causes tension in the Fe‐N(proximal His) bond, although the behaviour differs in detail from that of HbA(II)NO. There are two equilibrium states of Hbe having significantly different kinetics for the Hbe(III) Hbe(II) reaction of Hbe(III)NO. This autoreduction occurs in the form of two parallel processes, which collapse into one intermediate rate in the presence of Gri(2,3)P2. The temperature dependences of the rates enable deduction of H0 and S0 for the linked equilibrium, and yield liner Eyring plots for Hbe(III)NO, from which activation parameters were estimated on the basis of a previously described mechanism.
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Details
- Title
- Spectroscopic and kinetic aspects of Elephas maximus hemoglobin
- Creators
- Joseph J. Stephanos - Drexel UniversityAnthony W. Addison - Drexel University
- Publication Details
- European journal of biochemistry, v 189(1), pp 185-191
- Publisher
- Blackwell Publishing Ltd
- Number of pages
- 7
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:A1990DB21700022
- Scopus ID
- 2-s2.0-0025319835
- Other Identifier
- 991019173660904721
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- Web of Science research areas
- Biochemistry & Molecular Biology