Electrochemistry of Cytochrome P450 17α-Hydroxylase/17,20-Lyase (P450c17) | Sciact - CRIS-система Института катализа

Electrochemistry of Cytochrome P450 17α-Hydroxylase/17,20-Lyase (P450c17) Обзор

Конференция

XVIIth Adrenal Cortex Conference
29-31 мар. 2016 , Boston

Журнал

Molecular and Cellular Endocrinology
ISSN: 0303-7207 , E-ISSN: 1872-8057

Вых. Данные

Год: 2017, Том: 441, Страницы: 62-67 Страниц : 6 DOI: 10.1016/j.mce.2016.09.034

Ключевые слова

Adrenal cortex, Androgen, CYP17A1, Cytochrome P450c17, Direct electrochemistry, Electron transfer, Mechanism, Steroidogenesis

Авторы

Lisandra L.Martin ¹ , Kubeil Clemens ¹ , Simonov Alexandr N. ^1,6 , Kuznetsov Vladimir L. ² , Corbin C.Jo ³ , Auchus Richard J. ⁴ , Conley Alan J. ³ , Bond Alan M. ^1,6 , Rodgers Raymond J. ⁵

Организации

1	School of Chemistry, Monash University, Clayton, Victoria, 3800, Australia
2	Boreskov Institute of Catalysis, Prospekt Lavrentieva 5, Novosibirsk, 630090, Russia
3	School of Veterinary Medicine, University of California, Davis, CA, 95616, USA
4	Division of Metabolism, Endocrinology and Diabetes, Department of Internal Medicine, University of Michigan, Ann Arbor, MI, 48109, USA
5	Discipline of Obstetrics and Gynaecology, School of Medicine, Robinson Research Institute, University of Adelaide, Adelaide, South Australia, 5005, Australia
6	ARC Centre of Excellence for Electromaterials Science, Monash University, Clayton, Victoria, 3800, Australia

Информация о финансировании (2)

1	Australian Research Council
2	National Health and Medical Research Council

Within the superfamily of cytochrome P450 enzymes (P450s), there is a small class which is functionally employed for steroid biosynthesis. The enzymes in this class appear to have a small active site to accommodate the steroid substrates specifically and snuggly, prior to the redox transformation or hydroxylation to form a product. Cytochrome P450c17 is one of these and is also a multi-functional P450, with two activities, the first 17a-hydroxylation of pregnenolone is followed by a subsequent 17,20-lyase transformation to dehydroepiandrosterone (DHEA) as the dominant pathways to cortisol precursors or androgens in humans, respectively. How P450c17 regulates these two redox reactions is of special interest. There is a paucity of direct electrochemical studies on steroidogenic P450s, and in this minireview we provide an overview of these studies with P450c17. Historical consideration as to the difficulties in obtaining reliable electrochemistry due to issues of handling proteins on an electrode, together with advances in the electrochemical techniques are addressed. Recent work using Fourier transformed alternating current voltammetry is highlighted as this technique can provide both catalytic information simultaneously with the underlying redox transfer with the P450 haem.

Lisandra L.M. , Kubeil C. , Simonov A.N. , Kuznetsov V.L. , Corbin C.J. , Auchus R.J. , Conley A.J. , Bond A.M. , Rodgers R.J.
Electrochemistry of Cytochrome P450 17α-Hydroxylase/17,20-Lyase (P450c17)
Molecular and Cellular Endocrinology. 2017. V.441. P.62-67. DOI: 10.1016/j.mce.2016.09.034 WOS Scopus РИНЦ CAPlusCA PMID OpenAlex

Поступила в редакцию:	27 июн. 2016 г.
Принята к публикации:	30 сент. 2016 г.
Опубликована online:	3 окт. 2016 г.
Опубликована в печати:	5 февр. 2017 г.

Web of science:	WOS:000393247500009
Scopus:	2-s2.0-84991220460
РИНЦ:	29448363
Chemical Abstracts:	2016:1683996
Chemical Abstracts (print):	166:102719
PMID (PubMed):	27702589
OpenAlex:	W2529080109

БД	Цитирований
Web of science	4
Scopus	4
РИНЦ	4
OpenAlex	4