Iron:rusticyanin reductase

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Iron:rusticyanin reductase
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EC no. 1.16.9.1
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Iron:rusticyanin reductase (EC 1.16.9.1, Cyc2) is an enzyme with systematic name Fe(II):rusticyanin oxidoreductase. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

Fe(II) + rusticyanin Fe(III) + reduced rusticyanin

Rusticyanin reductase contains c-type heme.

Related Research Articles

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<i>Acidithiobacillus</i> Genus of bacteria

Acidithiobacillus is a genus of the Acidithiobacillia in the phylum "Pseudomonadota". This genus includes ten species of acidophilic microorganisms capable of sulfur and/or iron oxidation: Acidithiobacillus albertensis, Acidithiobacillus caldus, Acidithiobacillus cuprithermicus, Acidithiobacillus ferrianus, Acidithiobacillus ferridurans, Acidithiobacillus ferriphilus, Acidithiobacillus ferrivorans, Acidithiobacillus ferrooxidans, Acidithiobacillus sulfuriphilus, and Acidithiobacillus thiooxidans.A. ferooxidans is the most widely studied of the genus, but A. caldus and A. thiooxidans are also significant in research. Like all "Pseudomonadota", Acidithiobacillus spp. are Gram-negative and non-spore forming. They also play a significant role in the generation of acid mine drainage; a major global environmental challenge within the mining industry. Some species of Acidithiobacillus are utilized in bioleaching and biomining. A portion of the genes that support the survival of these bacteria in acidic environments are presumed to have been obtained by horizontal gene transfer.

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<span class="mw-page-title-main">Rusticyanin</span>

Rusticyanin (RCN) is a copper protein with a type I copper center that plays an integral role in electron transfer. It can be extracted from the periplasm of the gram-negative bacterium Thiobacillus ferrooxidans, also known as Acidithiobacillus ferrooxidans. Rusticyanin is also found in the membrane-bound form in the surface of T. ferrooxidans. It is a part of an electron transfer chain for Fe(II) oxidation.

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Acidithiobacillus caldus formerly belonged to the genus Thiobacillus prior to 2000, when it was reclassified along with a number of other bacterial species into one of three new genera that better categorize sulfur-oxidizing acidophiles. As a member of the Gammaproteobacteria class of Pseudomonadota, A. caldus may be identified as a Gram-negative bacterium that is frequently found in pairs. Considered to be one of the most common microbes involved in biomining, it is capable of oxidizing reduced inorganic sulfur compounds (RISCs) that form during the breakdown of sulfide minerals. The meaning of the prefix acidi- in the name Acidithiobacillus comes from the Latin word acidus, signifying that members of this genus love a sour, acidic environment. Thio is derived from the Greek word thios and describes the use of sulfur as an energy source, and bacillus describes the shape of these microorganisms, which are small rods. The species name, caldus, is derived from the Latin word for warm or hot, denoting this species' love of a warm environment.

<i>Acidithiobacillus thiooxidans</i> Species of bacterium

Acidithiobacillus thiooxidans, formerly known as Thiobacillus thiooxidans until its reclassification into the newly designated genus Acidithiobacillus of the Acidithiobacillia subclass of Pseudomonadota, is a Gram-negative, rod-shaped bacterium that uses sulfur as its primary energy source. It is mesophilic, with a temperature optimum of 28 °C. This bacterium is commonly found in soil, sewer pipes, and cave biofilms called snottites. A. thiooxidans is used in the mining technique known as bioleaching, where metals are extracted from their ores through the action of microbes.

References

  1. Blake RC, Shute EA (August 1994). "Respiratory enzymes of Thiobacillus ferrooxidans. Kinetic properties of an acid-stable iron:rusticyanin oxidoreductase". Biochemistry. 33 (31): 9220–8. doi:10.1021/bi00197a025. PMID   8049223.
  2. Appia-Ayme C, Bengrine A, Cavazza C, Giudici-Orticoni MT, Bruschi M, Chippaux M, Bonnefoy V (October 1998). "Characterization and expression of the co-transcribed cyc1 and cyc2 genes encoding the cytochrome c4 (c552) and a high-molecular-mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020". FEMS Microbiology Letters. 167 (2): 171–7. doi: 10.1111/j.1574-6968.1998.tb13224.x . PMID   9809418.
  3. Yarzábal A, Brasseur G, Ratouchniak J, Lund K, Lemesle-Meunier D, DeMoss JA, Bonnefoy V (January 2002). "The high-molecular-weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein". Journal of Bacteriology. 184 (1): 313–7. doi:10.1128/jb.184.1.313-317.2002. PMC   134758 . PMID   11741873.
  4. Yarzábal A, Appia-Ayme C, Ratouchniak J, Bonnefoy V (July 2004). "Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin". Microbiology. 150 (Pt 7): 2113–23. doi: 10.1099/mic.0.26966-0 . PMID   15256554.
  5. Taha TM, Kanao T, Takeuchi F, Sugio T (November 2008). "Reconstitution of iron oxidase from sulfur-grown Acidithiobacillus ferrooxidans". Applied and Environmental Microbiology. 74 (21): 6808–10. Bibcode:2008ApEnM..74.6808T. doi:10.1128/AEM.00787-08. PMC   2576702 . PMID   18791023.
  6. Castelle C, Guiral M, Malarte G, Ledgham F, Leroy G, Brugna M, Giudici-Orticoni MT (September 2008). "A new iron-oxidizing/O2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans". The Journal of Biological Chemistry. 283 (38): 25803–11. doi: 10.1074/jbc.M802496200 . PMC   3258861 . PMID   18632666.
  7. Quatrini R, Appia-Ayme C, Denis Y, Jedlicki E, Holmes DS, Bonnefoy V (August 2009). "Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans". BMC Genomics. 10: 394. doi: 10.1186/1471-2164-10-394 . PMC   2754497 . PMID   19703284.