R
Rick J. Krueger
Publications - 6
Citations - 574
Rick J. Krueger is an academic researcher. The author has contributed to research in topics: Siroheme & Ferredoxin. The author has an hindex of 6, co-authored 6 publications receiving 566 citations.
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Journal ArticleDOI
Acute adrenocorticotropic hormone stimulation of adrenal corticosteroidogenesis. Discovery of a rapidly induced protein.
Rick J. Krueger,N R Orme-Johnson +1 more
TL;DR: Two-dimensional electrophoretic techniques were used to identify and characterize a protein that is not produced in quiescent isolated rat adrenal cells but is produced in response to acute stimulation by adrenocorticotropic hormone (ACTH) or dibutyryl cAMP, and are consistent with p and i being related by cotranslational modification.
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Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase.
Rick J. Krueger,Lewis M. Siegel +1 more
TL;DR: Spinach SiR and nitrite reductase (NiR) both catalyze Fdr-or MV+-de-pendent six-electron reductions of SO3(2)- and NO2-, as well as the two electron reduction of NH2OH.
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Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism.
J R Lancaster,José M. Vega,Henry Kamin,N R Orme-Johnson,William H. Orme-Johnson,Rick J. Krueger,Lewis M. Siegel +6 more
TL;DR: EPR spectroscopic and chemical analyses of spinach nitrite reductase show that the enzyme contains one reducible iron-sulfur center, and one site for binding either cyanide or nitrite, per siroheme, indicating a role for the Fe4S4 center in catalysis.
Journal ArticleDOI
Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.
Lewis M. Siegel,D C Rueger,Michael J. Barber,Rick J. Krueger,N R Orme-Johnson,William H. Orme-Johnson +5 more
TL;DR: HP catalyzes stoichiometric 6-electron reductions of SO32- (to S2-) and of NO2- and of NH2OH, with reduced methyl viologen (MV+) as reductant, and binding of these ligands appears to be mutually exclusive and to involve the heme.