个人简介

BS Iowa State Univ. 1977, PhD Univ. Washington 1981, postdoctoral fellow, Northwestern University 1983, postdoctoral fellow, Univ. Minnesota 1983-1985.

研究领域

Inorganic Chemistry/Spectroscopic/Electrochemical and Theoretical Investigations of Metal Sites in Metalloproteins and Synthetic Model Systems Directed at Furthering the Understanding of Structure/Function Relationships in Biological or Catalytic Systems Involving Transition Metals

Research in my group involves using biophysical, molecular biological and synthetic model approaches to elucidate the structure of transition metal sites in proteins and enzymes, and investigate how these sites function in biology. We have focused our efforts on nickel biochemistry and redox systems involving S-donor ligands. Systems that are of current interest in my group include proteins involved in nickel trafficking, and several enzymes including hydrogenase, superoxide dismutase and cysteine dioxygenase. The wide variety of techniques that are used to investigate bioinorganic systems appeal to chemists earning degrees in biological, inorganic, organic and physical chemistry. Our research on Ni-containing hydrogenases illustrates this point. Hydrogenases are enzymes that catalyze the reversible two-electron oxidation of H2. As such, they are key enzymes in anaerobic microbial metabolism and have generated much interest as a possible means for producing and utilizing an alternative fuel. EPR studies of the hydrogenase isolated from the purple photosynthetic bacterium Thiocapsa roseopersicina demonstrated the presence an unusual redox-active Ni center that is involved in activating H2. X-ray absorption spectroscopy on the enzyme in various redox states reveals that the Ni is ligated by a combination of S- and N- or O-donor ligands. These studies also indicate that, although the EPR spectrum of the Ni site disappears and then reappears upon exposure to H2, the charge on the Ni atom does not change. Model studies directed at investigating the redox chemistry of Ni thiolate complexes suggest that much of the redox chemistry observed in hydrogenase involve the S-donor ligands (Figure). Sulfur-centered chemistry occurs naturally, and oxidation by O2 is the reaction that is catalyzed by cysteine dioxygenase in the conversion of cysteine to cysteine sulfinic acid. Hydrogenase must acquire nickel for activity, and this is accomplished via nickel-specific importers, metallochaperones and exporters that are regulated by nickel-specific transcription factors (Figure). How these trafficking proteins discriminate between metals and generate metal-specific biological responses is another aspect of the research.

近期论文

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Desguin, Benoit; Goffin, Philippe; Viaene, Eric; Kleerebezem, Michiel; Diaconescu Vlad M.; Maroney, Michael J.; Declercq, Jean-Paul; Soumillion, Patrice; Hols, Pascal. Lactate Racemase is a Nickel-dependent Enzyme Activated by a Widespread Maturation system. Nature communications 5 (2014). Dong, Jia; Joseph, Crisjoe A.; Borotto, Nicholas B.; Gill, Vanessa L.; Maroney,Michael J.; Vachet, Richard W. Unique Effect of Cu (II) in the Metal-Induced Amyloid Formation of 尾-2-Microglobulin. Biochemistry (2014), 53(8), 1263-1274. Zambelli, Barbara; Berardi, Andrea; Diaconescu, Vlad M.; Mazzei, Luca; Musiani, Francesco; Maroney, Michael J.; Ciurli, Stefano. Nickel Binding Properties of Helicobacter Pylori UreF, an Accessory Protein in the Nickel-based Activation of Urease. Journal of Biological Inorganic Chemistry (2014), 19(3), 319-334. Sheng, Yuewei; Abreu, Isabel A.; Cabelli, Diane E.; Maroney, Michael J.; Miller, Anne-Frances; Teixeira, Miguel; Valentine, Joan S. Superoxide Dismutases and Superoxide Reductases. Chemical Reviews (2014), 114(7), 3854-3918. Giri, Nitai Charan; Passantino, Lisa; Sun, Hong; Zoroddu, Maria Antonietta; Costa, Max; Maroney, Michael J. Structural Investigations of the Nickel-induced Inhibition of Truncated Constructs of the JMJD2 Family of Histone Demethylases Using X-ray Absorption Spectroscopy. Biochemistry (2013), 52(24), 4168-4183. Lisher, John P.; Higgins, Khadine A.; Maroney, Michael J.; Giedroc, David P. Physical Characterization of the Manganese-sensing Pneumococcal Surface Antigen Repressor from Streptococcus Pneumoniae. Biochemistry (2013), 52(43) 7689-7701. Maroney, Michael J. Enzymes: Nailing down hydrogenase. Nature Chemical Biology (2013), 9(1), 11-12. Ryan, Kelly C.; Maroney , Michael J.;Nickel Superoxide Dismutase. Encyclopedia of Metalloproteins (2013), 1505-1515. Maroney, Michael J.; Ciurli, Stefano. Nonredox Nickel Enzymes. Chemical reviews (2013), 114(8), 4206-4228. Fu, Yue; Ho-Ching, Tiffany Tsui; Bruce, Kevin E.; Sham, Lok-To; Higgins, Khadine A.; Lisher, John P.; Kazmierczak Krystyna M.; Maroney, Michael J.; Dann, Charles E. III; Winkler, Malcolm E.; Giedroc, David P. A New Structural Paradigm in Copper Resistance in Streptococcus Pneumoniae. Nature Chemical Biology (2013), 9(3), 177-183. Higgins, Khadine A.; Carr, Carolyn E.; Maroney, Michael J. Specific Metal Recognition in Nickel Trafficking. Biochemistry (2012), 51(40), 7816-7832. Flagg, Shannon C.; Giri, Nitai; Pektas, Serap; Maroney, Michael J. ; Knapp, Michael J. Inverse Solvent Isotope Effects Demonstrate Slow Aquo Release from Hypoxia Inducible Factor-Prolyl Hydroxylase (PHD2). Biochemistry (2012), 51(33), 6654-6666. Greene, Brandon L.; Joseph, Crisjoe A.; Maroney, Michael J. ; Dyer, R. Brian. Direct Evidence of Active-Site Reduction and Photodriven Catalysis in Sensitized Hydrogenase Assemblies. From Journal of the American Chemical Society, (2012), 134(27), 11108-11111. Higgins, Khadine A.; Chivers, Peter T.; Maroney, Michael J. Role of the N-terminus in determining metal-specific responses in the E. coli. Ni and Co responsive metalloregulator, RcnR. From Journal of the American Chemical Society (2012), 134(16), 7081-7093. Banaszak, Katarzyna; Martin-Diaconescu, Vlad; Bellucci, Matteo; Zambelli, Barbara; Rypniewski, Wojciech; Maroney, Michael J. ; Ciurli, Stefano. Crystallographic and X- ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveals a role for the disordered C- terminal arm in metal trafficking. Biochemical Journal (2012), 441(3), 1017-1026. Hosler, Erik R.; Herbst, Robert W.; Maroney, Michael J. ; Chohan, Balwant S. Exhaustive oxidation of a nickel dithiolate complex: some mechanistic insights en route to sukfate formation. Dalton Transactions (2012), 41(3), 804-816. Martin-Diaconescu, Vlad; Bellucci, Matteo; Musiani, Francesco; Ciurli, Stefano; Maroney, Michael J. Unraveling the Helicobacter pylori UreGzinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling. JBIC, Journal of Biological Inorganic Chemistry (2012), 17(3), 353-361. Giri, Nitai Charan; Sun, Hong; Chen, Hao-Bin; Costa, Max; Maroney, Michael J. XAS Structural Investigation of Early Intermediates in the Mechanism of DNA Repair by Human ABH2. Biochemistry (2011), 50(22), 5067-5076. Qian, Xinlei; Mester, Tuende; Morgado, Leonor; Arakawa, Tsutomu; Sharma, Manju L.; Inoue, Kengo; Joseph, Crisjoe; Salgueiro, Carlos A.; Maroney, Michael J.; Lovley, Derek R. Biochemical characterization of purified OmcS, a c-type cytochrome required for insoluble Fe(III) reduction in Geobacter sulfurreducens. Biochimica et Biophysica Acta, Bioenergetics (2011), 1807(4), 404-412. Herbst, Robert W.; Perovic, Iva; Martin-Diaconescu, Vlad; O'Brien, Kerrie; Chivers, Peter T.; Pochapsky, Susan Sondej; Pochapsky, Thomas C.; Maroney, Michael J.. Communication between the Zinc and Nickel Sites in Dimeric HypA: Metal Recognition and pH Sensing. Journal of the American Chemical Society (2010), 132(30), 10338-10351. Ryan, Kelly C.; Johnson, Olivia E.; Cabelli, Diane E.; Brunold, Thomas C.; Maroney, Michael J.. Nickel superoxide dismutase: structural and functional roles of Cys2 and Cys6. JBIC, Journal of Biological Inorganic Chemistry (2010), 15(5), 795-807. Johnson, Olivia E.; Ryan, Kelly C.; Maroney, Michael J.; Brunold, Thomas C. Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues. JBIC, Journal of Biological Inorganic Chemistry (2010),15(5), 777-793.