Literature DB >> 6268215

Hemoglobin-carbon monoxide binding rate. Low temperature magneto-optical detection of spin-tunneling.

M H Redi, B S Gerstman, J J Hopfield.   

Abstract

The spin-tunneling model of Hb--CO binding is used to calculate the binding rate at low temperature and high magnetic fields. The rate is calculated in second order perturbation theory assuming that spin-orbit coupling mediates the Hb iron electronic state change. The reaction which occurs at the crossing of the S = 2 and S = 0 energy vs. configuration coordinate curves is nonadiabatic, having a small electronic transition matrix element. Since detection of CO binding by polarized light in the Soret band makes it possible to observe hemes at specific orientation to the field direction, the rate is calculated for arbitrary heme orientation. Comparison with measurements at low temperature in zero field is made for spin quantization along the molecular crystal field direction.

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Year:  1981        PMID: 6268215      PMCID: PMC1327536          DOI: 10.1016/S0006-3495(81)84803-5

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  4 in total

1.  Electron transfer between biological molecules by thermally activated tunneling.

Authors:  J J Hopfield
Journal:  Proc Natl Acad Sci U S A       Date:  1974-09       Impact factor: 11.205

2.  Paramagnetic anisotropy measurements on a single crystal of deoxyhemoglobin.

Authors:  N Nakano; J Otsuka; A Tasaki
Journal:  Biochim Biophys Acta       Date:  1972-09-29

3.  Semiempirical calculations of model deoxyheme. Variation of calculated electromagnetic properties with electronic configuration and distance of iron from the plane.

Authors:  G H Loew; R F Kirchner
Journal:  Biophys J       Date:  1978-05       Impact factor: 4.033

4.  Molecular description of dioxygen bonding in hemoglobin.

Authors:  B D Olafson; W A Goddard
Journal:  Proc Natl Acad Sci U S A       Date:  1977-04       Impact factor: 11.205

  4 in total
  6 in total

1.  Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates.

Authors:  Xiong Ye; Dan Ionascu; Florin Gruia; Anchi Yu; Abdelkrim Benabbas; Paul M Champion
Journal:  Proc Natl Acad Sci U S A       Date:  2007-09-05       Impact factor: 11.205

2.  Photodissociation of CO and O2 from alpha and beta hemoglobin chains studied by using picosecond absorption spectroscopy.

Authors:  C R Guest; L J Noe
Journal:  Biophys J       Date:  1987-11       Impact factor: 4.033

3.  Picosecond absorption studies on the photodissociation of alpha- and beta-nitrosyl hemoglobin monomers.

Authors:  C R Guest; L J Noe
Journal:  Biophys J       Date:  1988-10       Impact factor: 4.033

4.  On the mechanism of ligand binding to myoglobin. The role of structural fluctuations.

Authors:  W Doster
Journal:  Eur Biophys J       Date:  1989       Impact factor: 1.733

5.  Measurements of heme relaxation and ligand recombination in strong magnetic fields.

Authors:  Zhenyu Zhang; Abdelkrim Benabbas; Xiong Ye; Anchi Yu; Paul M Champion
Journal:  J Phys Chem B       Date:  2009-08-06       Impact factor: 2.991

6.  Ultrafast CO Kinetics in Heme Proteins: Adiabatic Ligand Binding and Heavy Atom Tunneling.

Authors:  Abdelkrim Benabbas; Yuhan Sun; Thomas L Poulos; Paul M Champion
Journal:  J Am Chem Soc       Date:  2017-10-24       Impact factor: 15.419

  6 in total

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