Literature DB >> 6321478

Water coordination by heme iron in metmyoglobin.

J Peisach, W B Mims, J L Davis.   

Abstract

Using electron spin echo envelope spectroscopy, we have proven that the water close to heme in metmyoglobin is bound to the iron. For protein samples exchanged against D2O, we show that the electron nuclear coupling for 2H is 0.8 MHz. This coupling is considerably smaller in methemoglobin, pointing out a fundamental difference in bonding to water.

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Year:  1984        PMID: 6321478

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Coordination environment of a site-bound metal ion in the hammerhead ribozyme determined by 15N and 2H ESEEM spectroscopy.

Authors:  Matthew Vogt; Simanti Lahiri; Charles G Hoogstraten; R David Britt; Victoria J DeRose
Journal:  J Am Chem Soc       Date:  2006-12-27       Impact factor: 15.419

2.  Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex.

Authors:  P A Tipton; T P Quinn; J Peisach; P F Cook
Journal:  Protein Sci       Date:  1996-08       Impact factor: 6.725

3.  EPR and ENDOR studies of Fe(II) hemoproteins reduced and oxidized at 77 K.

Authors:  Roman Davydov; Brian M Hoffman
Journal:  J Biol Inorg Chem       Date:  2007-12-06       Impact factor: 3.358

  3 in total

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