METALLOPROTEINS FOR NITRIC OXIDE TRANSPORT AND OTHER ACTIVITIES

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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 program proposal for the study of five nitric oxide (NO) transport proteins called nitrophorins, and for a copper chaperone protein called CueO. NO is a ubiquitous signaling molecule in higher organisms and is of interest to medical and fundamental sciences. The nitrophorins are from two blood-sucking insects, Rhodnius prolixus (rNP1, rNP2, rNP4) and Cimex lectularius (cNP), and provide the best opportunity to date for understanding NO-heme interactions in proteins. We have crystal structures of rNP1, rNP2, and rNP4, and good crystals of cNP and CueO. The proposal is for ultrahigh resolution studies of rNP4 (to 0.8 ¿¿, structure determinations of NO complexes with all of the nitrophorins and their mutant forms, freeze trapping experiments with NP4, which undergoes a large conformational change in the crystal, and MAD experiments for cNP and CueO. The shorter wavelengths available at the synchrotron are required for the NO complex structure determinations, due to photodissociation or photoreduction affects that occur with Cu K-alpha radiation.