Editing Catalase (section)

== Distribution among organisms ==
The large majority of known organisms use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]] in mammals.<ref>{{cite journal| vauthors = Ilyukha VA | journal=Journal of Evolutionary Biochemistry and Physiology | title = Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis |date=2001|volume=37|issue=3|pages=241–245|doi=10.1023/A:1012663105999| s2cid=38916410 }}</ref> Catalase is found primarily in [[peroxisome]]s and the [[cytosol]] of [[erythrocyte]]s (and sometimes in [[mitochondria]]<ref name="pmid11351128">{{cite journal | vauthors = Bai J, Cederbaum AI | title = Mitochondrial catalase and oxidative injury | journal = Biological Signals and Receptors | volume = 10 | issue = 3–4 | pages = 189–199 | year = 2001 | pmid = 11351128 | doi = 10.1159/000046887 | s2cid = 33795198 }}</ref>)

Almost all [[aerobic microorganisms]] use catalase. It is also present in some [[Anaerobic organism|anaerobic]] [[microorganisms]], such as ''[[Methanosarcina barkeri]]''.<ref name="pmid16735730">{{cite journal | vauthors = Brioukhanov AL, Netrusov AI, Eggen RI | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri | journal = Microbiology | volume = 152 | issue = Pt 6 | pages = 1671–1677 | date = June 2006 | pmid = 16735730 | doi = 10.1099/mic.0.28542-0 | doi-access = free }}</ref> Catalase is also universal among [[plants]] and occurs in most [[fungi]].<ref>{{cite journal | vauthors = Hansberg W, Salas-Lizana R, Domínguez L | title = Fungal catalases: function, phylogenetic origin and structure | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 170–180 | date = September 2012 | pmid = 22698962 | doi = 10.1016/j.abb.2012.05.014 }}</ref>

One unique use of catalase occurs in the [[bombardier beetle]]. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.<ref name="pmid10449758">{{cite journal | vauthors = Eisner T, Aneshansley DJ | title = Spray aiming in the bombardier beetle: photographic evidence | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 17 | pages = 9705–9709 | date = August 1999 | pmid = 10449758 | pmc = 22274 | doi = 10.1073/pnas.96.17.9705 | bibcode = 1999PNAS...96.9705E | doi-access = free }}</ref> The oxidation reaction is very [[exothermic]] (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.<ref name="Beheshti_2006">{{cite journal|vauthors=Beheshti N, McIntosh AC|year=2006|title=A biomimetic study of the explosive discharge of the bombardier beetle|url=http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|url-status=dead|journal=International Journal of Design & Nature|volume=1|issue=1|pages=1–9|archive-url=https://web.archive.org/web/20110726145856/http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|archive-date=2011-07-26}}</ref>

Long-lived queens of the [[termite]] ''[[Reticulitermes]] speratus'' have significantly lower [[DNA oxidation|oxidative damage to their DNA]] than non-reproductive individuals (workers and soldiers).<ref name="pmid28076409">{{cite journal | vauthors = Tasaki E, Kobayashi K, Matsuura K, Iuchi Y | title = An Efficient Antioxidant System in a Long-Lived Termite Queen | journal = PLOS ONE | volume = 12 | issue = 1 | pages = e0167412 | date = 2017 | pmid = 28076409 | pmc = 5226355 | doi = 10.1371/journal.pone.0167412 | doi-access = free | bibcode = 2017PLoSO..1267412T }}</ref>  Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.<ref name="pmid28076409" />  It appears that the efficient [[antioxidant]] capability of termite queens can partly explain how they attain longer life.

Catalase enzymes from various species have vastly differing optimum temperatures. [[Poikilotherm]]ic animals typically have catalases with optimum temperatures in the range of 15-25&nbsp;°C, while mammalian or avian catalases might have optimum temperatures above 35&nbsp;°C,<ref name="mits56" /><ref name="imm03">{{cite journal| vauthors = Çetinus ŞA, Öztop HN |title=Immobilization of catalase into chemically crosslinked chitosan beads|journal=Enzyme and Microbial Technology|date=June 2003|volume=32|issue=7|pages=889–894|doi=10.1016/S0141-0229(03)00065-6}}</ref> and catalases from plants vary depending on their [[growth habit]].<ref name="mits56">{{cite journal| vauthors = Mitsuda H |title=Studies on Catalase|journal=Bulletin of the Institute for Chemical Research, Kyoto University|date=1956-07-31|volume=34|issue=4|pages=165–192|url=https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf |archive-url=https://ghostarchive.org/archive/20221009/https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf |archive-date=2022-10-09 |url-status=live|access-date=27 September 2017}}</ref> In contrast, catalase isolated from the [[hyperthermophile]] [[archaeon]] ''[[Pyrobaculum calidifontis]]'' has a temperature optimum of 90&nbsp;°C.<ref name="pmid12029047">{{cite journal | vauthors = Amo T, Atomi H, Imanaka T | title = Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 | journal = Journal of Bacteriology | volume = 184 | issue = 12 | pages = 3305–3312 | date = June 2002 | pmid = 12029047 | pmc = 135111 | doi = 10.1128/JB.184.12.3305-3312.2002 }}</ref>