Russell Lobrutto
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Senior Research Scientist, received his Ph.D. in Biophysics at the State University of New York (SUNY) at Buffalo. After postdoctoral studies at SUNY/Albany and at the University of Pennsylvania, Dr. LoBrutto was appointed Assistant Professor of Physics at Northeastern University in Boston. He joined the ASU Plant Biology Department in September of 1991.
The principal focus of our work is the use of state-of-the-art electron paramagnetic resonance (EPR) methodology to measure important structural features of metalloenzymes and other metal-utilizing proteins. Most of our studies involve either electron transport complexes (especially in photosynthesis), or enzymes that utilize coenzymes and other cofactors. One common class of cofactor is the metal ion or cluster (e.g. iron-sulfur), which becomes EPR-active by virtue of a half-integer total spin S in certain redox states. Also amenable to EPR detection and analysis are many enzymes that form free radicals as they react. These radicals can have unpaired electron spin density concentrated upon the protein itself, or on a coenzyme.
The broad family of EPR techniques can be applied to studies of protein structure and function in many ways, but one particularly valuable approach is to measure the magnetic couplings between unpaired electron spins and neighboring non-zero spin nuclei. The strengths and characteristics of these couplings can, in the best cases, reveal metal-ligand or metal-near neighbor distances, as well as the nature of the chemical moiety containing the metal-coordinating atom (e.g., the identity of the amino acid residue which provides a ligand). We are equipped to measure electron-nuclear hyperfine couplings by use of both continuous-wave (CW) EPR and the more sophisticated pulsed microwave methods such as electron spin echo envelope modulation (ESEEM) and pulsed electron-nuclear double resonance (ENDOR).
We are engaged in collaborative work with other members of the School of Life Sciences, as well as with several investigators in the Department of Chemistry and Biochemistry. In addition, the EPR facility has attracted collaborative projects to ASU from distinguished biochemists at universities and research institutes nationwide.
Selected Publications
Barney, Brett M., Matthew R.Schaab, Russell LoBrutto, and Wilson A. Francisco (2004) "Evidence for a new metal in a known active site: purification and characterization of an iron-containing quercetin 2,3-dioxygenase from Bacillus subtilis." Protein Expression and Purification 35 , 131-141.
Laura L Eggink, Russell LoBrutto, Daniel C Brune, Judy Brusslan, Akihiro Yamasato, Ayumi Tanaka, and J. Kenneth Hoober (2004). "Synthesis of chlorophyll b : localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit." BMC Plant Biology 4 :5.
Caudle MT*, CK. Mobley , LM Bafaro, R LoBrutto, GT. Yee, and TL Groy. (2004). EPR and magnetic properties of heteronuclear MnnMg6-n(O2CNEt2)12: Impact of structural distortions on Mn(II) in weak ligand fields. Inorg. Chem. 43(2), 506-514.
Kalman, L.; LoBrutto, R.; Narvaez, A. J.; Williams, J. C.; Allen, J. P.; (2003) Correlation of Proton Release and Electrochromic Shifts of the Optical Spectrum Due to Oxidation of Tyrosine in Reaction Centers from Rhodobacter sphaeroides Biochemistry 42(45) 13280-13286.
Kalman, L, LoBrutto R, Allen, JP, Williams, JC (2003) Manganese Oxidation by Modified Reaction Centers from Rhodobacter Sphaeroides, Biochemistry 42(37); 11016-11022.
Schwartz P, R LoBrutto, GH Reed, and PA Frey. (2003) Suicide inactivation of dioldehydrase by 2-chloroacetaldehyde: Formation of the 'cis-ethanesemidione' radical, and the role of a monovalent cation. Helvetica Chimica Acta 86 (11): 3764-3775.
Narvaez AJ, Kalman L, LoBrutto R, Allen JP, Williams JC (2002) Influence of the protein environment on the properties of a tyrosyl radical in reaction centers from Rhodobacter sphaeroides, Biochemistry41(51), 15253-15258.
Smith, T. S., II, LoBrutto, R., and Pecoraro, V. L. (2002) Paramagnetic Spectroscopy of Vanadyl Complexes and its Applications to Biological Systems. Coordin Chem Rev 228 (1): 1-18.
Crampton, DJ, R LoBrutto, and WD Frasch. (2001). Identification of the P-Loop Lysine as a metal ligand in the absence of nucleotide at catalytic site 3 of chloroplast F1-ATPase from Chlamydomonas reinhardtii. Biochemistry 40(12):3710-3716.
Kabil, O, S Taoka, R LoBrutto, R Shoemaker, and R Banerjee. (2001). The Pyridoxal Phosphate binding sites are similar in human heme-dependent and yeast heme-independent cystathionine beta-synthases. Evidence from 31P NMR and pulsed EPR spectroscopy that the heme and PLP cofactors are not proximal in the human enzyme. J Biol Chem 276(22):19350-19355.
LoBrutto, R, V Bandarian, O Th Magnusson, X.Chen, VL Schramm, and GH Reed. (2001). 5'-Deoxyadenosine Contacts the Substrate Radical Intermediate in the Active Site of Ethanolamine Ammonia-lyase: 2H and 13C Electron Nuclear Double Resonance Studies. Biochemistry 40:9-14.
Chang, C-W T, DA Johnson, V Bandarian, H Zhou, R LoBrutto, GH Reed, and H-W Liu. (2000). Characterization of a Unique Coenzyme B6 Radical in the Ascarylose Biosynthetic Pathway. J Am Chem Soc 122(17):4239-4240.
Kalman, L, R LoBrutto, JP Allen, and JC Williams. (1999). Modified Reaction Centres Oxidize Tyrosine in Reactions that Mirror Photosystem II. Nature 402:696-699.
Chen, W, R LoBrutto, and WD Frasch. (1999). EPR Spectroscopy of VO2+-ATP bound to catalytic site 3 of chloroplast F1-ATPase from Chlamydomonas reveals changes in metal ligation resulting from mutations to the phosphate-binding loop Threonine (betaT168). J Biol Chem 274:7089-7094.
LoBrutto, R, BJ Hamstra, GJ Colpas, VL Pecoraro, and WD Frasch. (1998). ESEEM Spectroscopy Reveals and Distinguishes Equatorial and Axial Nitrogen Ligands Bound to VO2+. J Am Chem Soc 120:4410-4416.