NMR Studies of the Dynamics of High-Spin Nitrophorins: Comparative Studies of NP4 and NP2 at Close to Physiological pH.
Biochemistry. 2014 Dec 8;
Authors: Berry RE, Muthu D, Yang F, Walker FA
Abstract
The ?-barrel nitrophorin (NP) heme proteins are found in the saliva of the blood-sucking insect Rhodnius prolixus, which synthesizes and stores nitric oxide (NO) in the salivary glands. NO is bound to iron of the NPs and is released by dilution and pH rise when the insect spits its saliva into the tissues of a victim, to aid in obtaining a blood meal. In the adult insect there are four ni-trophorins, NP1 - NP4, which have sequence similarities in two pairs, NP1/NP4 (90% identical) and NP2/NP3 (80% identical). The NP4 crystal structures available have been used to propose that pH-dependent changes in conformation of two loops between adjacent ?-strands at the front opening of the protein, the A-B and G-H loops, determine the rate of NO release. At pH 7.3, NP4 releases NO 17 times faster than does NP2. In this work, the aqua complexes of NP4 and NP2 have been investigated by NMR relaxation measurements to probe the pico- to nanosecond and micro- to millisecond timescale motions at two pH values, 6.5 and 7.3. It is found that NP4-OH2 is fairly rigid and only residues in the loop regions show dynamics at pH 6.5, while at pH 7.3 much more dynamics of the loops and most of the ?-strands is observed, while the ?-helices remain fairly rigid. In comparison, NP2-OH2 shows much less dynamics, albeit somewhat more than the previously-reported NP2-NO complex (Muthu, D.; Berry, R. E.; Zhang, H.; Walker, F. A. (2013) Biochemistry 52, 7910-7925). The reasons for this major difference between NP4 and NP2 are discussed.
PMID: 25486224 [PubMed - as supplied by publisher]
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NMR Studies of the Dynamics of High-Spin Nitrophorins: Comparative Studies of NP4 and NP2 at Close to Physiological pH.
Linear Mode
