This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This is a 2-year proposal for APS beam time for structural studies of biological macromolecules. It focuses on the mammalian serine protease thrombin, on two flavoprotein redox systems and on electron transfer (ET) mutants of a cupredoxin that accepts electrons from a quinoenzyme. Human thrombin catalyzes the proteolytic conversion of fibrinogen to fibrin, the major component of a blood clot. The structures of several mutant forms of these proteins, as well as of various enzyme-substrate and enzyme-inhibitor complexes will be determined in order to elucidate their modes of action. These studies will be extended to the murine enzyme which differs in several respects from the human enzyme. One of the redox flavoproteins, heterotetrameric sarcosine oxidase (TSOX), isolated from Pseudomonas maltophilia, contains FAD, FMN and binds tetrahydrofolate (THF). TSOX catalyzes the oxidation of sarcosine (N-methyl glycine) to an imine intermediate and reduced FAD;in a second step the imine intermediate combines with THF to form 5,10-methylene-THF. The two catalytic sites are separated by about 35 A. The FAD is reoxidized by ET to FMN and the latter then reduces molecular oxygen to yield peroxide. A second redox flavoenzyme is nikD, which catalyzes an early step in the biosynthesis of nikkomycin antibiotics in Streptomyces tendae. It is a monomer of 45 kDa containing FAD;its structure is known in two distinct conformation. Structures of its mutants will be studied. Amicyanin is a blue copper protein of 9 kDa that accepts electrons from methylamine dehydrogenase (MADH) in Paracoccus denitrificans. The redox properties of several amicyanin mutants show significant differences from the wild type protein;atomic resolution structures of these mutants are known. Crystals of ET complexes of these mutants with MADH will be studied.
| Weingarten, Adam S; Dannenhoffer, Adam J; Kazantsev, Roman V et al. (2018) Chromophore Dipole Directs Morphology and Photocatalytic Hydrogen Generation. J Am Chem Soc 140:4965-4968 |
| Yang, Cheolhee; Choi, Minseo; Kim, Jong Goo et al. (2018) Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Int J Mol Sci 19: |
| Kazantsev, Roman V; Dannenhoffer, Adam J; Weingarten, Adam S et al. (2017) Crystal-Phase Transitions and Photocatalysis in Supramolecular Scaffolds. J Am Chem Soc 139:6120-6127 |
| Fournier, Bertrand; Sokolow, Jesse; Coppens, Philip (2016) Analysis of multicrystal pump-probe data sets. II. Scaling of ratio data sets. Acta Crystallogr A Found Adv 72:250-60 |
| Cho, Hyun Sun; Schotte, Friedrich; Dashdorj, Naranbaatar et al. (2016) Picosecond Photobiology: Watching a Signaling Protein Function in Real Time via Time-Resolved Small- and Wide-Angle X-ray Scattering. J Am Chem Soc 138:8815-23 |
| Pande, Kanupriya; Hutchison, Christopher D M; Groenhof, Gerrit et al. (2016) Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein. Science 352:725-9 |
| Weingarten, Adam S; Kazantsev, Roman V; Palmer, Liam C et al. (2015) Supramolecular Packing Controls H? Photocatalysis in Chromophore Amphiphile Hydrogels. J Am Chem Soc 137:15241-6 |
| Pfoh, Roland; Pai, Emil F; Saridakis, Vivian (2015) Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides. Acta Crystallogr D Biol Crystallogr 71:2032-9 |
| Mariette, Céline; Guérin, Laurent; Rabiller, Philippe et al. (2015) The creation of modulated monoclinic aperiodic composites in n-alkane/urea compounds. Z Kristallogr Cryst Mater 230:5-11 |
| Yang, Xiaojing; Stojkovi?, Emina A; Ozarowski, Wesley B et al. (2015) Light Signaling Mechanism of Two Tandem Bacteriophytochromes. Structure 23:1179-89 |
Showing the most recent 10 out of 120 publications
