Serge N. Vinogradov, Ph.D.

My research interests center on the physical and chemical properties of nonvertebrate hemoglobins, which, unlike vertebrate hemoglobins, exhibit a wide variation in their covalent and subunit structures as well as several orders of magnitude greater variation in ligand binding affinities and kinetics. The giant, extracellular hemoglobins of annelids and deep-sea vestimentiferans are large (~3.5 MDa) complexes of globin and nonglobins, characterized by a hexagonal bilayer electron microscopic appearance. Several of these have been characterized by a variety of biophysical techniques ranging from sedimentation equilibrium, scanning transmission mass mapping, to three-dimensional reconstruction from cryoelectron microscopic images and electrospray ionization mass spectrometry. Furthermore, their dissociations at extremes of pH and at neutral pH in the presence of detergent and denaturants have been investigated. A common quaternary structure was found, consisting of twelve subassemblies, each comprised of twelve globin chains tethered to a central subassembly of thirty-six linker chains. The reassembly of the hexagonal bilayer structure requires the presence of linker chains and calcium.

Suzuki, T., S.N. Vinogradov. Amino acid sequences of globin and linker chains from the giant, hexagonal bilayer hemoglobin of the leech Macrobdella decora: phylogenetic relationship to other annelid sequences. J Protein Chem., in press.

Green, B.N., F. Zal, F.H. Lallier, A. Toulmond, T. Suzuki, T. Gotoh, S.N. Vinogradov. Observation of large, noncovalent globin subassemblies in the ~3600 kDa hexagonal bilayer hemoglobins by electrospray ionization time-of-flight mass spectrometry. J. Mol. Biol. 309:553-560, 2001.

Weber, R.E., S.N. Vinogradov. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol. Rev. 81:568-629, 2001.

Kuchumov, A.R., J.A. Loo, S.N. Vinogradov. Subunit distribution of calcium binding sites in the 3.6 MDa hexagonal bilayer hemoglobin from Lumbricus terrestris. J. Protein Chem. 19:139-149, 2000.

Lamy,J., A. R. Kuchumov, J-C. Taveau, N. Boisset, S. N. Vinogradov, J. N. Lamy. Reassembly of Lumbricus terrestris hemoglobin: a study by matrix-assisted laser desorption/ ionization mass spectrometry and 3D reconstruction from frozen-hydrated specimens. J. Mol. Biol. 298:633-647, 2000.

Green, B.N., R.S. Bordoli, L.G. Hanin, F.H. Lallier, A. Toulmond, S.N. Vinogradov. Electrospray ionization mass spectrometric determination of the molecular mass of the ~200kDa globin dodecamer subassemblies in hexagonal bilayer hemoglobins. J. Biol. Chem. 274:28206-28212, 1999.

Kuchumov, A.R., J.-C. Taveau, J.N. Lamy, J. S. Wall, R.E. Weber, S.N. Vinogradov. The role of the linker subunits in the reassembly of the 3.6MDa hexagonal bilayer hemoglobin from Lumbricus terrestris. J. Mol. Biol. 289:1361-1374, 1999.