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

Basilio Zafrilla; Rosa María Martínez‑Espinosa; Mari­a José Bonete; Julea N. Butt; David J. Richardson; Andrew J. Gates

doi:10.1042/BST20110709

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

Basilio Zafrilla, Rosa María Martínez‑Espinosa, Maria José Bonete, Julea N. Butt, David J. Richardson, Andrew J. Gates

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Abstract

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.

Original language	English
Pages (from-to)	1844-1848
Number of pages	5
Journal	Biochemical Society Transactions
Volume	39
Issue number	6
DOIs	https://doi.org/10.1042/BST20110709
Publication status	Published - 2011

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10.1042/BST20110709

Cite this

@article{efb418dc924f415da66e9f24ec94b0fd,

title = "A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation",

abstract = "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.",

author = "Basilio Zafrilla and Mart{\'i}nez‑Espinosa, {Rosa Mar{\'i}a} and Bonete, {Maria Jos{\'e}} and Butt, {Julea N.} and Richardson, {David J.} and Gates, {Andrew J.}",

year = "2011",

doi = "10.1042/BST20110709",

language = "English",

volume = "39",

pages = "1844--1848",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

number = "6",

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TY - JOUR

T1 - A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation

AU - Zafrilla, Basilio

AU - Martínez‑Espinosa, Rosa María

AU - Bonete, Maria José

AU - Butt, Julea N.

AU - Richardson, David J.

AU - Gates, Andrew J.

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

U2 - 10.1042/BST20110709

DO - 10.1042/BST20110709

M3 - Article

VL - 39

SP - 1844

EP - 1848

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 6

ER -