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Year Number of Results
1954 1
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1963 1
1965 5
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1967 4
1968 2
1970 2
1972 2
1973 2
1975 4
1976 14
1977 11
1978 8
1979 8
1980 13
1981 8
1982 14
1983 7
1984 13
1985 8
1986 12
1987 13
1988 8
1989 10
1990 15
1991 18
1992 15
1993 28
1994 20
1995 21
1996 22
1997 24
1998 28
1999 28
2000 24
2001 26
2002 41
2003 31
2004 42
2005 46
2006 39
2007 30
2008 35
2009 37
2010 27
2011 35
2012 40
2013 23
2014 28
2015 25
2016 23
2017 22
2018 24
2019 20
2020 29
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2024 3

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Page 1
Heme A biosynthesis.
Hederstedt L. Hederstedt L. Biochim Biophys Acta. 2012 Jun;1817(6):920-7. doi: 10.1016/j.bbabio.2012.03.025. Epub 2012 Mar 30. Biochim Biophys Acta. 2012. PMID: 22484221 Free article. Review.
Heme A synthase catalyzes the formation of the formyl side group and is a poorly understood heme-containing membrane bound atypical monooxygenase. This review presents our current understanding of heme A synthesis at the molecular level in mitochondria …
Heme A synthase catalyzes the formation of the formyl side group and is a poorly understood heme-containing membrane bound aty …
Heme, Heme Oxygenase-1, Statins, and SARS-CoV-2.
Stevenson DK, Vreman HJ, Wong RJ. Stevenson DK, et al. Antioxidants (Basel). 2023 Mar 2;12(3):614. doi: 10.3390/antiox12030614. Antioxidants (Basel). 2023. PMID: 36978862 Free PMC article.
Heme, a metalloporphyrin, or more specifically, a tetrapyrrole containing ferrous iron, is an ancient molecule [...]....
Heme, a metalloporphyrin, or more specifically, a tetrapyrrole containing ferrous iron, is an ancient molecule [...]....
Isolated Heme A Synthase from Aquifex aeolicus Is a Trimer.
Zeng H, Zhu G, Zhang S, Li X, Martin J, Morgner N, Sun F, Peng G, Xie H, Michel H. Zeng H, et al. mBio. 2020 Jun 30;11(3):e02615-19. doi: 10.1128/mBio.02615-19. mBio. 2020. PMID: 32605991 Free PMC article.
The integral membrane protein heme A synthase (HAS) catalyzes the biosynthesis of heme A, which is a prerequisite for cellular respiration in a wide range of aerobic organisms. ...It plays a key role in oxygen reduction by serving as an electron carrie …
The integral membrane protein heme A synthase (HAS) catalyzes the biosynthesis of heme A, which is a prerequisit …
Pleiotropic effects of statins.
Kavalipati N, Shah J, Ramakrishan A, Vasnawala H. Kavalipati N, et al. Indian J Endocrinol Metab. 2015 Sep-Oct;19(5):554-62. doi: 10.4103/2230-8210.163106. Indian J Endocrinol Metab. 2015. PMID: 26425463 Free PMC article. Review.
Statins or 3-hydroxy-methylglutaryl coenzyme A (HMG CoA) reductase inhibitors not only prevents the synthesis of cholesterol biosynthesis but also inhibits the synthesis of essential isoprenoid intermediates such as farnesyl pyrophosphate, geranylgeranyl pyrophosphate, isopentany …
Statins or 3-hydroxy-methylglutaryl coenzyme A (HMG CoA) reductase inhibitors not only prevents the synthesis of cholesterol biosynthesis bu …
Individual heme a and heme a(3) contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase.
Diuba AV, Vygodina TV, Azarkina NV, Arutyunyan AM, Soulimane T, Vos MH, Konstantinov AA. Diuba AV, et al. Biochim Biophys Acta Bioenerg. 2023 Apr 1;1864(2):148937. doi: 10.1016/j.bbabio.2022.148937. Epub 2022 Nov 18. Biochim Biophys Acta Bioenerg. 2023. PMID: 36403793 Free article.
The resolved spectra show splitting of the electronic B(0x)-, B(0y)-transitions of both reduced hemes. The heme a(2+) spectrum is shifted to the red relative to heme a(3)(2+) spectrum. The 425 nm shoulder is mostly attributed to heme a(3) …
The resolved spectra show splitting of the electronic B(0x)-, B(0y)-transitions of both reduced hemes. The heme a(2+) spectrum …
Calcium-bound structure of bovine cytochrome c oxidase.
Muramoto K, Shinzawa-Itoh K. Muramoto K, et al. Biochim Biophys Acta Bioenerg. 2023 Apr 1;1864(2):148956. doi: 10.1016/j.bbabio.2023.148956. Epub 2023 Jan 25. Biochim Biophys Acta Bioenerg. 2023. PMID: 36708913 Free article.
The crystal structure of bovine cytochrome c oxidase (CcO) shows a sodium ion (Na(+)) bound to the surface of subunit I. Changes in the absorption spectrum of heme a caused by calcium ions (Ca(2+)) are detected as small red shifts, and inhibition of enzymatic activi …
The crystal structure of bovine cytochrome c oxidase (CcO) shows a sodium ion (Na(+)) bound to the surface of subunit I. Changes in the abso …
Effect of Ca(2+) on the redox potential of heme a in cytochrome c oxidase.
Vygodina TV, Kaminskaya OP, Konstantinov AA, Ptushenko VV. Vygodina TV, et al. Biochimie. 2018 Jun;149:71-78. doi: 10.1016/j.biochi.2018.04.005. Epub 2018 Apr 7. Biochimie. 2018. PMID: 29635042
Here we show that binding of Ca(2+) at CBS of bovine CcO shifts E(m) of heme a to the positive by 15-20 mV. Na(+) ions that bind to the same site and compete with Ca(2+) do not affect E(m) of heme a and also prevent and reverse the effect of Ca(2+). No …
Here we show that binding of Ca(2+) at CBS of bovine CcO shifts E(m) of heme a to the positive by 15-20 mV. Na(+) ions that bi …
Biosynthesis and trafficking of heme o and heme a: new structural insights and their implications for reaction mechanisms and prenylated heme transfer.
Rivett ED, Heo L, Feig M, Hegg EL. Rivett ED, et al. Crit Rev Biochem Mol Biol. 2021 Dec;56(6):640-668. doi: 10.1080/10409238.2021.1957668. Epub 2021 Aug 25. Crit Rev Biochem Mol Biol. 2021. PMID: 34428995 Free PMC article. Review.
The majority of these terminal oxidases contain a prenylated heme (typically heme a or occasionally heme o) in the active site. In addition, many heme-copper oxidases, including mitochondrial cytochrome c oxidases, possess a second heme a cofactor. Des …
The majority of these terminal oxidases contain a prenylated heme (typically heme a or occasionally heme o) in the active site …
Allosteric Cooperativity in Proton Energy Conversion in A1-Type Cytochrome c Oxidase.
Capitanio G, Palese LL, Papa F, Papa S. Capitanio G, et al. J Mol Biol. 2020 Jan 17;432(2):534-551. doi: 10.1016/j.jmb.2019.09.027. Epub 2019 Oct 15. J Mol Biol. 2020. PMID: 31626808 Review.
Cytochrome c oxidase (CcO), the Cu(A,) heme a, heme a(3), Cu(B) enzyme of respiratory chain, converts the free energy released by aerobic cytochrome c oxidation into a membrane electrochemical proton gradient (deltamuH(+)). deltamuH(+) derives from the …
Cytochrome c oxidase (CcO), the Cu(A,) heme a, heme a(3), Cu(B) enzyme of respiratory chain, converts the free e …
Diversity of Cytochrome c Oxidase Assembly Proteins in Bacteria.
Hederstedt L. Hederstedt L. Microorganisms. 2022 Apr 28;10(5):926. doi: 10.3390/microorganisms10050926. Microorganisms. 2022. PMID: 35630371 Free PMC article. Review.
Using the model organisms Bacillus subtilis, Corynebacterium glutamicum, Paracoccus denitrificans, and Rhodobacter sphaeroides, the present review focuses on proteins for assembly of the heme a, heme a(3), Cu(B), and Cu(A) metal centers. The known bios …
Using the model organisms Bacillus subtilis, Corynebacterium glutamicum, Paracoccus denitrificans, and Rhodobacter sphaeroides, the present …
1,032 results