Abstract

The autotrophic bacterium, Nitrosomonas europaea, derives energy from the oxidation of ammonia to nitrite. Oxidation of the intermediate, hydroxylamine, is catalyzed by hydroxylamine oxidoreductase. Electrons pass from this enzyme to the tetraheme cytochrome c-554. This cytochrome is thought to direct some electrons to an electron transfer chain leading to ATP-synthesis. The four hemes in cytochrome c-554 are magnetically coupled, giving rise to a single unusual EPR feature. The goal of NMR studies is to elucidate details of this magnetic coupling. The studies are aimed at determining (a) the axial ligands of the hemes, (b) the nature of amino acid groups that interact with the hemes and (c) possible interactions between hemes. NOESY spectra with different mixing times (30, 50, 70 and 80 msec), one-dimensional NOE spectra and a COSY spectrum have been recorded. We have concluded that unambiguous assignments are not possible for the oxidized protein with unlabeled hemes because of difficulties in distinguishing intra- and interheme connectivities.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002301-12
Application #
5223948
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

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Dominguez, Eddie; Zarnowski, Robert; Sanchez, Hiram et al. (2018) Conservation and Divergence in the Candida Species Biofilm Matrix Mannan-Glucan Complex Structure, Function, and Genetic Control. MBio 9:
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Wales, Jessica A; Chen, Cheng-Yu; Breci, Linda et al. (2018) Discovery of stimulator binding to a conserved pocket in the heme domain of soluble guanylyl cyclase. J Biol Chem 293:1850-1864
Selen Alpergin, Ebru S; Bolandnazar, Zeinab; Sabatini, Martina et al. (2017) Metabolic profiling reveals reprogramming of lipid metabolic pathways in treatment of polycystic ovary syndrome with 3-iodothyronamine. Physiol Rep 5:
Mong, Surin K; Cochran, Frank V; Yu, Hongtao et al. (2017) Heterochiral Knottin Protein: Folding and Solution Structure. Biochemistry 56:5720-5725

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