Modulating the nitrite reductase activity of globins by varying the heme substituents: Utilizing myoglobin as a model system. | Academic Article individual record
abstract

Globins, such as hemoglobin (Hb) and myoglobin (Mb), have gained attention for their ability to reduce nitrite (NO2(-)) to nitric oxide (NO). The molecular interactions that regulate this chemistry are not fully elucidated, therefore we address this issue by investigating one part of the active site that may control this reaction. Here, the effects of the 2,4-heme substituents on the nitrite reductase (NiR) reaction, and on the structures and energies of the ferrous nitrite intermediates, are investigated using Mb as a model system. This is accomplished by studying Mbs with hemes that have different 2,4-R groups, namely diacetyldeuteroMb (-acetyl), protoMb (wild-type (wt) Mb, -vinyl), deuteroMb (-H), and mesoMb (-ethyl). While trends on the natural charge on Fe and O-atom of bound nitrite are observed among the series of Mbs, the Fe(II)-NPyr (Pyr=pyrrole) and Fe(II)-NHis93 (His=histidine) bond lengths do not significantly change. Kinetic analysis shows increasing NiR activity as follows: diacetyldeuteroMb

authors
publication outlet

J Inorg Biochem

author list (cited authors)
Galinato, M., Fogle, R. S., Stetz, A., & Galan, J. F
publication date
2016
publisher
Elsevier bv Publisher
keywords
  • Protein Binding
  • Nitrite Reductases
  • Heme
  • Nitric Oxide
  • Oxidation-Reduction
  • Myoglobin
  • Nitrites
  • Kinetics
  • Reduction
  • Models, Chemical
  • Horses
  • Density Functional Theory
  • Animals
  • Nitrite
  • Quantum Theory
  • Models, Molecular
citation count

6

PubMed ID
26544504
identifier
375604SE
Digital Object Identifier (DOI)
start page
7
end page
20
volume
154