A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation.

نویسندگان

  • Basilio Zafrilla
  • Rosa María Martínez-Espinosa
  • María José Bonete
  • Julea N Butt
  • David J Richardson
  • Andrew J Gates
چکیده

In the absence of ammonium, many organisms, including the halophilic archaeon Haloferax volcanii DS2 (DM3757), may assimilate inorganic nitrogen from nitrate or nitrite, using a ferredoxin-dependent assimilatory NO₃⁻/NO₂⁻ reductase pathway. The small acidic ferredoxin Hv-Fd plays an essential role in the electron transfer cascade required for assimilatory nitrate and nitrite reduction by the cytoplasmic NarB- and NirA-type reductases respectively. UV-visible absorbance and EPR spectroscopic characterization of purified Hv-Fd demonstrate that this protein binds a single [2Fe-2S] cluster, and potentiometric titration reveals that the cluster shares similar redox properties with those present in plant-type ferredoxins.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A composite biochemical system for bacterial nitrate and nitrite assimilation as exemplified by Paracoccus denitrificans.

The denitrifying bacterium Paracoccus denitrificans can grow aerobically or anaerobically using nitrate or nitrite as the sole nitrogen source. The biochemical pathway responsible is expressed from a gene cluster comprising a nitrate/nitrite transporter (NasA), nitrite transporter (NasH), nitrite reductase (NasB), ferredoxin (NasG) and nitrate reductase (NasC). NasB and NasG are essential for g...

متن کامل

Nitrite-responsive activation of the nitrate assimilation operon in Cyanobacteria plays an essential role in up-regulation of nitrate assimilation activities under nitrate-limited growth conditions.

NtcB of the cyanobacterium Synechococcus elongatus strain PCC 7942 is a LysR family protein that enhances expression of the nitrate assimilation operon (nirA operon) in response to the presence of nitrite, an intermediate of assimilatory nitrate reduction. Inactivation of ntcB in this cyanobacterium specifically abolishes the nitrite responsiveness of nirA operon expression, but under nitrate-r...

متن کامل

A novel variant of ferredoxin-dependent sulfite reductase having preferred substrate specificity for nitrite in the unicellular red alga Cyanidioschyzon merolae.

Plant NiR (nitrite reductase) and SiR (sulfite reductase) have common structural and functional features. Both enzymes are generally distinguished in terms of substrate specificity for nitrite and sulfite. The genome of Cyanidioschyzon merolae, a unicellular red alga living in acidic hot springs, encodes two SiR homologues, namely CmSiRA and CmSiRB (C. merolae sulfite reductases A and B), but n...

متن کامل

Isolation of a rice regeneration quantitative trait loci gene and its application to transformation systems.

Regeneration of plant organs is often the essential step in genetic transformation; however, the regeneration ability of a plant varies depending on the genetic background. By conventional crosses of low-regeneration rice strain Koshihikari with high-regeneration rice strain Kasalath, we identified some quantitative trait loci, which control the regeneration ability in rice. Using a map-based c...

متن کامل

Reevaluation of "ammonium

The intermediate role of hydroxylamine in nitrate assimilation has been suggested by observations that different organisms form ammonia from hydroxylamine in vivo, and that hydroxylamine occurs in nutrient media and cells. In further support are recent investigations describing enzymatic preparations which catalyze the reduction of hydroxylamine to ammonia. Taniguchi et al. (J. Biochem. (Japan)...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical Society transactions

دوره 39 6  شماره 

صفحات  -

تاریخ انتشار 2011