Substrate-Dependent Mechanism Switch in the Desaturation Reactions of the Mononuclear Nonheme Iron Enzyme PtlD

基质(水族馆) 动力学同位素效应 碳阳离子 羟基化 脱质子化 化学 光化学 立体化学 氢原子萃取 激进的 有机化学 物理 量子力学 离子 海洋学 地质学
作者
Linyue Chen,Qian Deng,Tingting Ma,Jiayue Gu,Juan Yang,Xuan Zhang,You‐Quan Zou,Zixin Deng,Li Chen,Changming Zhao
出处
期刊:ACS Catalysis [American Chemical Society]
卷期号:14 (10): 7389-7401 被引量:5
标识
DOI:10.1021/acscatal.4c00757
摘要

PtlD, a multifunctional mononuclear nonheme iron and α-ketoglutarate-dependent (NHFe/α-KG) dioxygenase involved in neopentalenoketolactone biosynthesis, catalyzes hydroxylation, desaturation, and olefin epoxidation reactions. Investigating desaturation reactions of nonactivated carbons mediated by NHFe/α-KG enzymes is intriguing, especially for understanding the fate of the substrate radicals formed after hydrogen atom abstraction by FeIV═O species. Here, we investigate the desaturation reaction mechanism of PtlD using two distinct substrates: neopentalenolactone D (1) features a lone pair-containing oxygen atom adjacent to the olefin-forming carbon atoms, whereas pentalenolactone D (7) harbors a carbonyl group at the corresponding position. For substrate 1, our isotope effect measurement and protein mutagenesis experiments suggest the formation of a carbocation intermediate, which is subsequently deprotonated by a base to generate the desaturation products. Residue K288 serves as the base, while Y113 likely stabilizes the carbocation via a π-cation interaction. For substrate 7, oxygen incorporation patterns indicated that a carbocation intermediate is also formed but is unstable, leading to hydroxylation due to H2O quenching. Notably, substrate 7's desaturation exhibits a temperature-dependent large kinetic isotope effect (KIE) and an inverse solvent isotope effect (SIE), suggesting that hydrogen tunneling contributes to the electron–proton transfer (EPT) process. These findings collectively reveal the cases of NHFe/α-KG enzymes, where distinct desaturation mechanisms switch with different substrates.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
PDF的下载单位、IP信息已删除 (2025-6-4)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
谢琉圭发布了新的文献求助10
2秒前
wu发布了新的文献求助10
3秒前
打滚完成签到,获得积分10
4秒前
LJJ发布了新的文献求助10
4秒前
睡觉了完成签到 ,获得积分10
6秒前
量子星尘发布了新的文献求助10
7秒前
乖猫要努力应助精明寻梅采纳,获得10
7秒前
AI完成签到,获得积分10
10秒前
xiaosu发布了新的文献求助30
11秒前
11秒前
谢琉圭完成签到,获得积分10
13秒前
领导范儿应助稳重的若雁采纳,获得10
16秒前
16秒前
17秒前
wu完成签到,获得积分20
17秒前
momo发布了新的文献求助10
18秒前
19秒前
田様应助123采纳,获得10
19秒前
23秒前
zying完成签到,获得积分10
26秒前
27秒前
双楠应助wangjue采纳,获得10
27秒前
32秒前
雪白尔岚发布了新的文献求助10
36秒前
36秒前
36秒前
慕青应助momo采纳,获得10
37秒前
从容冰夏完成签到,获得积分10
39秒前
39秒前
桐桐应助Candy采纳,获得10
40秒前
YR完成签到,获得积分10
42秒前
欧阳月空发布了新的文献求助10
42秒前
周em12_发布了新的文献求助10
43秒前
糊涂涂完成签到 ,获得积分10
43秒前
44秒前
46秒前
Zhang完成签到,获得积分10
47秒前
48秒前
48秒前
高分求助中
A new approach to the extrapolation of accelerated life test data 1000
ACSM’s Guidelines for Exercise Testing and Prescription, 12th edition 500
‘Unruly’ Children: Historical Fieldnotes and Learning Morality in a Taiwan Village (New Departures in Anthropology) 400
Indomethacinのヒトにおける経皮吸収 400
Phylogenetic study of the order Polydesmida (Myriapoda: Diplopoda) 370
基于可调谐半导体激光吸收光谱技术泄漏气体检测系统的研究 350
Robot-supported joining of reinforcement textiles with one-sided sewing heads 320
热门求助领域 (近24小时)
化学 材料科学 医学 生物 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 遗传学 基因 物理化学 催化作用 冶金 细胞生物学 免疫学
热门帖子
关注 科研通微信公众号,转发送积分 3989334
求助须知:如何正确求助?哪些是违规求助? 3531428
关于积分的说明 11253936
捐赠科研通 3270119
什么是DOI,文献DOI怎么找? 1804887
邀请新用户注册赠送积分活动 882087
科研通“疑难数据库(出版商)”最低求助积分说明 809173