Abstract:
:Marinobacter hydrocarbonoclasticus nitric oxide reductase, cNOR, is an integral membrane protein composed of two subunits with different roles, NorC (electron transfer) and NorB (catalytic) that receives electrons from the soluble cytochrome c552 and reduces nitric oxide to nitrous oxide in the denitrification pathway. The solvent-exposed domain of NorC, harboring a c-type heme was heterologously produced, along with its physiological electron donor, cytochrome c552. These two proteins were spectroscopically characterized and shown to be similar to the native proteins, both being low-spin and Met-His coordinated, with the soluble domain of NorC presenting some additional features of a high-spin heme, which is consistent with the higher solvent accessibility of its heme and weaker coordination of the methionine axial ligand. The electron transfer complex between the two proteins has a 1:1 stoichiometry, and an upper limit for the dissociation constant was estimated by 1H NMR titration to be 1.2±0.4μM. Electrochemical techniques were used to characterize the interaction between the proteins, and a model structure of the complex was obtained by molecular docking. The electrochemical observations point to the modulation of the NorC reduction potential by the presence of NorB, tuning its ability to receive electrons from cytochrome c552.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Ramos S,Almeida RM,Cordas CM,Moura JJG,Pauleta SR,Moura Idoi
10.1016/j.jinorgbio.2017.09.001subject
Has Abstractpub_date
2017-12-01 00:00:00pages
402-411eissn
0162-0134issn
1873-3344pii
S0162-0134(17)30368-9journal_volume
177pub_type
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