ABSTRACT
This chapter summarizes the recent work on nitrosylheme proteins (nitrophorins) from bloodsucking insects, to survey the known interactions of nitric oxide (NO) with heme proteins, including comparisons and contrasts between the nitrophorins and other systems. It also summarizes the physical and spectroscopic methods utilized for characterizing the structure, bonding, and reactivity of heme-NO complexes in general. The saliva of bloodsucking arthropods contains a vast array of substances that counteract blood coagulation, platelet function, and vasoconstriction of their hosts. These substances allow bloodsucking arthropods to minimize the time taken for a blood meal. The chapter summarizes the spectroscopic, crystallographic, kinetic, and redox investigations that have been carried out on model hemes, hemoglobin, myoglobin, cytochrome a3 of cytochrome oxidase, horseradish peroxidase, prostaglandin H synthase, cytochromes P450, chloroperoxidase, and so forth have shown us the unique properties of heme-NO centers.
