Ma, K., Hutchins, A., Sung, S.J. and Adams, M.W.W. (1997) Pyruvate Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon, Pyrococcus furiosus, Functions as a CoA-Dependent Pyruvate Decarboxylase. Proceedings of the National Academy of Sciences of the United States of America, 94, 9608-9613.
http://dx.doi.org/10.1073/pnas.94.18.9608

has been cited by the following article:

• TITLE: Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis

  AUTHORS: Yukiko Ozawa, Yasufumi Umena, Takeo Imai, Yukio Morimoto

  KEYWORDS: Oxidoreductase, X-Ray Analysis, Iron-Sulfur Cluster

  JOURNAL NAME: Advances in Enzyme Research, Vol.3 No.3, September 8, 2015

  ABSTRACT: 2-ketoisovalerate ferredoxin oxidoreductase (VOR) is a key enzyme in hyperthermophiles catalyzing the coenzyme A-dependent oxidative decarboxylation of aliphatic amino acid-derived 2-keto acids. The enzyme purified under anaerobic conditions from a hyperthermophilic archaeon, Thermococcus profundus, is a hetero-octamer (αβγδ)2 consisting of four different subunits, α = 45 kDa, β = 31 kDa, γ = 22 kDa and δ = 13 kDa, respectively, and it has three [4Fe-4S] clusters per αβγδ-protomer, similar to other ferredoxin oxidoreductases. In the present study, the native enzyme was purified from this strain and crystallized to give rod-like crystals that were suitable for X-ray diffraction experiments. The crystals belonged to space group P41212, with unit-cell parameters a = b = 136.20 Å, c = 221.07 Å. Diffraction images were processed to a resolution of 3.0 Å. The data collected so far indicate the approximate molecular boundaries and a partial main-chain trace of the enzyme.