Title | Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | Vanwetswinkel, S., N. A. J. van Nuland, and A. Volkov |
Journal | J Biomol NMR |
Volume | 57 |
Issue | 1 |
Pagination | 21-6 |
Date Published | 2013 Sep |
ISSN | 1573-5001 |
Abstract | Here we describe paramagnetic NMR analysis of the low- and high-spin forms of yeast cytochrome c peroxidase (CcP), a 34 kDa heme enzyme involved in hydroperoxide reduction in mitochondria. Starting from the assigned NMR spectra of a low-spin CN-bound CcP and using a strategy based on paramagnetic pseudocontact shifts, we have obtained backbone resonance assignments for the diamagnetic, iron-free protein and the high-spin, resting-state enzyme. The derived chemical shifts were further used to determine low- and high-spin magnetic susceptibility tensors and the zero-field splitting constant (D) for the high-spin CcP. The D value indicates that the latter contains a hexacoordinate heme species with a weak field ligand, such as water, in the axial position. Being one of the very few high-spin heme proteins analyzed in this fashion, the resting state CcP expands our knowledge of the heme coordination chemistry in biological systems. |
DOI | 10.1007/s10858-013-9760-8 |
Alternate Journal | J. Biomol. NMR |
PubMed ID | 23832496 |
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