[HTML][HTML] Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex

J Simon, R Eichler, R Pisa, S Biel, R Gross - FEBS letters, 2002 - Elsevier
The two multiheme c-type cytochromes NrfH and NrfA form a membrane-bound complex that
catalyzes menaquinol oxidation by nitrite during respiratory nitrite ammonification of …

Crystal structure of Azotobacter cytochrome c5 at 2.5 Å resolution

DC Carter, KA Melis, SE O'Donnell, BK Burgess… - Journal of molecular …, 1985 - Elsevier
The crystal structure of cytochrome c 5 from Azotobacter vinelandii has been solved and
refined to an R value of 0.29 at 2.5 Å resolution. The structure of the oxidized protein was …

Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea

R Timkovich, D Bergmann, DM Arciero, AB Hooper - Biophysical journal, 1998 - cell.com
Cytochrome c-552 from Nitrosomonas europaea is a 9.1-kDa monoheme protein that is a
member of the bacterial cytochrome c-551 family. The gene encoding for c-552 has been …

Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobactercapsulatus

TH Tahirov, S Misaki, TE Meyer, MA Cusanovich… - nature structural …, 1996 - nature.com
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus
cytochrome c′. This is the first example of a ligand-bound structure of a class Ha …

Cytochrome P460 of Nitrosomonas europaea: Formation of the heme‐lysine cross‐link in a heterologous host and mutagenic conversion to a non‐cross‐linked …

DJ Bergmann, AB Hooper - European journal of biochemistry, 2003 - Wiley Online Library
The heme of cytochrome P460 of Nitrosomonas europaea, which is covalently crosslinked to
two cysteines of the polypeptide as with all c‐type cytochromes, has an additional novel …

X‐ray structure of the membrane‐bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination

ML Rodrigues, TF Oliveira, IAC Pereira… - The EMBO journal, 2006 - embopress.org
Oxidation of membrane‐bound quinol molecules is a central step in the respiratory electron
transport chains used by biological cells to generate ATP by oxidative phosphorylation. A …

Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri determined at 2.2 Å resolution

A Kadziola, S Larsen - Structure, 1997 - cell.com
Background: Cytochromes c 4 are dihaem cytochromes c found in a variety of bacteria. They
are assumed to take part in the electron-transport systems associated with both aerobic and …

Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms

Y Matsuura, T Takano, RE Dickerson - Journal of molecular biology, 1982 - Elsevier
The molecular structures of ferri-and ferrocytochrome c 551 from Pseudomonas aeruginosa
have been refined at a resolution of 1.6 Å, to an R factor of 19.5% for the oxidized molecule …

[HTML][HTML] Cytochromes P460 and c′-beta; a new family of high-spin cytochromes c

BO Elmore, DJ Bergmann, MG Klotz, AB Hooper - FEBS letters, 2007 - Elsevier
Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and
the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of …

Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner

P Cedervall, AB Hooper, CM Wilmot - Biochemistry, 2013 - ACS Publications
Hydroxylamine oxidoreductase (HAO) is a 24-heme homotrimeric enzyme that catalyzes the
conversion of hydroxylamine to nitrite in nitrifying bacteria: a key reaction in the nitrogen …