Electrochemistry of Cytochrome P450 17α-Hydroxylase/17,20-Lyase (P450c17)
Обзор
| Общее |
Язык:
Английский,
Жанр:
Обзор (Review),
Статус опубликования:
Опубликована,
Оригинальность:
Оригинальная
|
| 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.