@article{fdi:010044142,
  title = {{B}iochemical and spectroscopic characterization of the membrane-bound nitrate reductase from {M}arinobacter hydrocarbonoclasticus 617},
  author = {{C}orreia, {C}. and {B}esson, {S}. and {B}rondino, {C}. {D}. and {G}onzalez, {P}. {J}. and {F}auque, {G}uy and {L}ampreia, {J}. and {M}oura, {I}. and {M}oura, {J}. {J}. {G}.},
  editor = {},
  language = {{ENG}},
  abstract = {{M}embrane-bound nitrate reductase from {M}arinobacter hydrocarbonoclasticus 617 can be solubilized in either of two ways that will ultimately determine the presence or absence of the small ({I}) subunit. {T}he enzyme complex ({N}ar{GHI}) is composed of three subunits with molecular masses of 130, 65, and 20 k{D}a. {T}his enzyme contains approximately 14 {F}e, 0.8 {M}o, and 1.3 molybdopterin guanine dinucleotides per enzyme molecule. {C}uriously, one heme b and 0.4 heme c per enzyme molecule have been detected. {T}hese hemes were potentiometrically characterized by optical spectroscopy at p{H} 7.6 and two noninteracting species were identified with respective midpoint potentials at {E}-m = + 197 m{V} (heme c) and-4.5 m{V} (heme b). {V}ariable-temperature (4-120 {K}) {X}-band electron paramagnetic resonance ({EPR}) studies performed on both as-isolated and dithionite-reduced nitrate reductase showed, respectively, an {EPR} signal characteristic of a [3{F}e-4{S}](+) cluster and overlapping signals associated with at least three types of [4{F}e-4{S}](+) centers. {EPR} of the as-isolated enzyme shows two distinct p{H}-dependent {M}o({V}) signals with hyperfine coupling to a solvent-exchangeable proton. {T}hese signals, called "lowp{H}' and "high-p{H},' changed to a p{H}-independent {M}o({V}) signal upon nitrate or nitrite addition. {N}itrate addition to dithionite-reduced samples at p{H} 6 and 7.6 yields some of the {EPR} signals described above and a new rhombic signal that has no hyperfine structure. {T}he relationship between the distinct {EPR}-active {M}o({V}) species and their plausible structures is discussed on the basis of the structural information available to date for closely related membrane-bound nitrate reductases.},
  keywords = {{N}itrate reductase ; {E}lectron paramagnetic resonance ; {M}olybdenum ; {D}enitrification ; {M}arinobacter hydrocarbonoclasticus},
  booktitle = {},
  journal = {{J}ournal of {B}iological {I}norganic {C}hemistry},
  volume = {13},
  numero = {8},
  pages = {1321--1333},
  ISSN = {0949-8257},
  year = {2008},
  DOI = {10.1007/s00775-008-0416-1},
  URL = {https://www.documentation.ird.fr/hor/fdi:010044142},
}