Research Topics
Genomes and Genes | CATHERINE DRENNANSummaryAffiliation: Massachusetts Institute of Technology Country: USA Publications
Research Grants
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Publications
The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in picturesCatherine L Drennan
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
J Biol Inorg Chem 9:511-5. 2004....
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenaseC L Drennan
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Proc Natl Acad Sci U S A 98:11973-8. 2001..The two Rossmann domains contribute ligands to the active site C-cluster. This x-ray structure provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems...- Surprising cofactors in metalloenzymesCatherine L Drennan
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA
Curr Opin Struct Biol 13:220-6. 2003.... - A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthaseTzanko I Doukov
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Science 298:567-72. 2002.... - Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzymeFrederick Berkovitch
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Science 303:76-9. 2004..The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments... - Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesisLeah C Blasiak
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Nature 440:368-71. 2006..6 A resolution. This structure reveals a previously unknown coordination of iron, in which the carboxylate ligand of the facial triad is replaced by a chloride ion... - Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzymeLuke J Higgins
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Nature 437:838-44. 2005.... - The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimerMichael D Sintchak
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Nat Struct Biol 9:293-300. 2002..Thus, L. leichmannii RNR is a paradigm for the simplest structural entity capable of ribonucleotide reduction, a reaction linking the RNA and DNA worlds... - Structural analysis of an open active site conformation of nonheme iron halogenase CytC3Cintyu Wong
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, Massachusetts 02139, USA
J Am Chem Soc 131:4872-9. 2009.... - Bringing the excitement of biological research into the chemistry classroom at MITElizabeth Vogel Taylor
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
ACS Chem Biol 2:515-7. 2007 - Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebCKatherine S Ryan
Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
Proc Natl Acad Sci U S A 104:15311-6. 2007.... 
The violacein biosynthetic enzyme VioE shares a fold with lipoprotein transporter proteinsKatherine S Ryan
Department of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
J Biol Chem 283:6467-75. 2008..This structural and mutagenesis study suggests that VioE acts as a catalytic chaperone, using a fold previously associated with lipoprotein transporters to catalyze the production of its prodeoxyviolacein product...- Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthaseYan Kung
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 48:7432-40. 2009..The crystal structures presented here, along with recent structures of CODHs from other organisms, have led us toward a unified mechanism for CO oxidation by the C-cluster, the catalytic center of an environmentally important enzyme... - First-principles study of non-heme Fe(II) halogenase SyrB2 reactivityHeather J Kulik
Department of Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
J Am Chem Soc 131:14426-33. 2009.... - Ribbon-helix-helix transcription factors: variations on a themeEric R Schreiter
Department of Chemistry and Protein Research Center, University of Puerto Rico at Rio Piedras, San Juan, Puerto Rico 00931, Puerto Rico
Nat Rev Microbiol 5:710-20. 2007.... - A research-inspired laboratory sequence investigating acquired drug resistanceElizabeth Vogel Taylor
Departments of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Biochem Mol Biol Educ 38:247-52. 2010..The exercises provide students with a hands-on understanding of the impact of biochemistry on human health, and demonstrate their potential as the next generation of investigators... - The FAD cofactor of RebC shifts to an IN conformation upon flavin reductionKatherine S Ryan
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 47:13506-13. 2008..Along with kinetic data presented here, these structures suggest that the first cycle of catalysis in RebC may resemble that of p-hydroxybenzoate hydroxylase, with substrate binding promoting flavin reduction... - Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coliChristine M Phillips
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 49:7830-8. 2010.... - NikR-operator complex structure and the mechanism of repressor activation by metal ionsEric R Schreiter
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Proc Natl Acad Sci U S A 103:13676-81. 2006.... - Structural perspective on enzymatic halogenationLeah C Blasiak
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Acc Chem Res 42:147-55. 2009.... - Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthaseTzanko I Doukov
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 47:3474-83. 2008.... - Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzymeJessica L Vey
Departments of Chemistry and Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
Proc Natl Acad Sci U S A 105:16137-41. 2008.... - Physical basis of metal-binding specificity in Escherichia coli NikRChristine M Phillips
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
J Am Chem Soc 131:10220-8. 2009..Taken together, these data suggest that the EcNikR structure is most stable when Ni(2+) occupies high-affinity sites and that EcNikR binding to DNA is more favorable when the second site contains K(+)... - Thioredoxin reductase from Thermoplasma acidophilum: a new twist on redox regulationHector H Hernandez
Department of Chemistry, Massachusetts Institute of Technology, 16 573, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA
Biochemistry 47:9728-37. 2008..Our discovery of a TrxR that does not use NADPH provides a new twist in redox regulation... - Structural basis of the metal specificity for nickel regulatory protein NikRChristine M Phillips
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 47:1938-46. 2008..These structural findings along with biochemical data on NikR support a hypothesis that ordering of the alpha3 helix is important for repressor activation... - A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutaseFrederick Berkovitch
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
Proc Natl Acad Sci U S A 101:15870-5. 2004..Thus, the structure embodies a locking mechanism to keep the adenosylcobalamin out of the active site and prevent radical generation in the absence of substrate... - Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduriaPaul A Hubbard
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
J Biol Chem 282:31308-16. 2007.... - Searching for the Nik operon: how a ligand-responsive transcription factor hunts for its DNA binding siteChristine M Phillips
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Biochemistry 49:7757-63. 2010..coli NikR and the cellular model for transcription factors in general, are in agreement, and the details laid out by the NikR system may lend additional credence to the current models for transcription factors searching for DNA... - Crystal structure of the nickel-responsive transcription factor NikREric R Schreiter
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139 USA
Nat Struct Biol 10:794-9. 2003..The regulatory domain of NikR contains four nickel-binding sites at the tetramer interface, each exhibiting a novel square-planar coordination by three histidines and one cysteine side chain... - AdoMet radical proteins--from structure to evolution--alignment of divergent protein sequences reveals strong secondary structure element conservationYvain Nicolet
Department of Chemistry 16-573, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
Nucleic Acids Res 32:4015-25. 2004..These differences in barrel architecture also explain how AdoMet radical enzymes can act on substrates that range in size from 10 atoms to 608 residue proteins... - Direct electrochemical analyses of a thermophilic thioredoxin reductase: interplay between conformational change and redox chemistryMichael J Hamill
Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, USA
Biochemistry 47:9738-46. 2008.... - Direct electrochemical characterization of archaeal thioredoxinsSarah E Chobot
Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA
Angew Chem Int Ed Engl 46:4145-7. 2007 - Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803Bhramara Tirupati
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA
Biochemistry 43:12210-9. 2004.... - Structures of the iron-sulfur flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidusSusana L A Andrade
Institut fur Mikrobiologie und Genetik, Abt Molekulare Strukturbiologie, Georg August Universitat Gottingen, Justus von Liebig Weg 11, 37077 Gottingen, Germany
J Bacteriol 187:3848-54. 2005..This is only possible between different monomers upon oligomerization. Fundamental differences in the surface properties of the two ISF homologs underscore the diversity encountered within this protein family... - Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferasesTzanko I Doukov
Department of Biochemistry, Beadle Center, University of Nebraska, Lincoln, Nebraska 68588 0664, USA
J Biol Chem 282:6609-18. 2007.... - Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenasesEllen Yeh
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA
Biochemistry 46:1284-92. 2007..This covalent enzyme chloramine likely plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes...
Research Grants
- Complex Metallocluster Structure and AssemblyCATHERINE DRENNAN; Fiscal Year: 2009..Our goals are to explore the mechanism and assembly of complex metallocofactors, as well as the cellular regulation of nickel uptake and iron-sulfur cluster biogenesis. ..
- X-ray studies of metalloenzyme regulation and catalysisCATHERINE DRENNAN; Fiscal Year: 2007..We will complement structural data with biochemical characterization and single crystal spectroscopic techniques. ..
- Complex Metallocluster Structure and AssemblyCATHERINE DRENNAN; Fiscal Year: 2007..To explore cellular Ni uptake, we will investigate the structure and mechanism of Ni-regulatory protein NikR. ..
- SUMMER RESEARCH IN MACROMOLECULAR INTERACTIONSCATHERINE DRENNAN; Fiscal Year: 2004..The proposed training project complements institutional goals of expanding career choices for students majoring in physical and quantitative sciences, and increasing minority participation in undergraduate research programs. ..
- Complex Metallocluster Structure and AssemblyCatherine L Drennan; Fiscal Year: 2010..Our goals are to explore the mechanism and assembly of complex metallocofactors, as well as the cellular regulation of nickel uptake and iron-sulfur cluster biogenesis. ..