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High-Resolution Structures of the Oxidized and Reduced States of Cytochrome c554 from Nitrosomonas europaea

Iverson, Tina M. and Arciero, David M. and Hooper, Alan B. and Rees, Douglas C. (2001) High-Resolution Structures of the Oxidized and Reduced States of Cytochrome c554 from Nitrosomonas europaea. Journal of Biological Inorganic Chemistry, 6 (4). pp. 390-397. ISSN 0949-8257. doi:10.1007/s007750100213.

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Cytochrome c554 (cyt c554) is a tetra-heme cytochrome involved in the oxidation of NH3 by Nitrosomonas europaea. The X-ray crystal structures of both the oxidized and dithionite-reduced states of cyt c554 in a new, rhombohedral crystal form have been solved by molecular replacement, at 1.6 Å and 1.8 Å resolution, respectively. Upon reduction, the conformation of the polypeptide chain changes between residues 175 and 179, which are adjacent to hemes III and IV. Cyt c554 displays conserved heme-packing motifs that are present in other heme-containing proteins. Comparisons to hydroxylamine oxidoreductase, the electron donor to cyt c554, and cytochrome c nitrite reductase, an enzyme involved in nitrite ammonification, reveal substantial structural similarity in the polypeptide chain surrounding the heme core environment. The structural determinants of these heme-packing motifs extend to the buried water molecules that hydrogen bond to the histidine ligands to the heme iron. In the original structure determination of a tetragonal crystal form, a cis peptide bond between His129 and Phe130 was identified that appeared to be stabilized by crystal contacts. In the rhombohedral crystal form used in the present high-resolution structure determination, this peptide bond adopts the trans conformation, but with disallowed angles of φ and ψ.

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Rees, Douglas C.0000-0003-4073-1185
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Additional Information:© 2001 SBIC. Received 27 October 2000; Accepted 11 January 2001; Published online 28 March 2011. We thank R. Dieckmann, J. Chiu, and F.A. Tezcan for experimental assistance and J.A. Shelnutt for calculations of the distortions of the porphyrins. This work was supported by an NSF grant (MCB-9723608) to A.B.H. and an NIH grant (GM45162) to D.C.R. T.M.I. was supported by an NIH fellowship (GM07737). This work is based upon research conducted at the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the Department of Energy, Office of Basic Energy Sciences.
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Department of Energy (DOE)UNSPECIFIED
Subject Keywords:cytochrome; heme; nitrification; porphyrin; Nitrosomonas europaea
Issue or Number:4
Record Number:CaltechAUTHORS:20150108-153416410
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ID Code:53404
Deposited By: SWORD User
Deposited On:08 Feb 2015 06:40
Last Modified:10 Nov 2021 20:01

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