PMID- 32227866
OWN - NLM
STAT- MEDLINE
DCOM- 20210412
LR  - 20210412
IS  - 1520-4898 (Electronic)
IS  - 0001-4842 (Linking)
VI  - 53
IP  - 4
DP  - 2020 Apr 21
TI  - Structural Insight into [NiFe] Hydrogenase Maturation by Transient Complexes 
      between Hyp Proteins.
PG  - 875-886
LID - 10.1021/acs.accounts.0c00022 [doi]
AB  - [NiFe] hydrogenases catalyze reversible hydrogen production/consumption. The core 
      unit of [NiFe] hydrogenase consists of a large and a small subunit. The active 
      site of the large subunit of [NiFe] hydrogenases contains a NiFe(CN)(2)CO 
      cluster. The biosynthesis/maturation of these hydrogenases is a complex and 
      dynamic process catalyzed primarily by six Hyp proteins (HypABCDEF), which play 
      central roles in the maturation process. HypA and HypB are involved in the Ni 
      insertion, whereas HypC, D, E, and F are required for the biosynthesis, assembly, 
      and insertion of the Fe(CN)(2)CO group. HypE and HypF catalyze the synthesis of 
      the CN group through the carbamoylation and cyanation of the C-terminus cysteine 
      of HypE. HypC and HypD form a scaffold for the assembly of the Fe(CN)(2)CO 
      moiety.Over the last decades, a large number of biochemical studies on maturation 
      proteins have been performed, revealing basic functions of each Hyp protein and 
      the overall framework of the maturation pathway. However, it is only in the last 
      10 years that structural insight has been gained, and our group has made 
      significant contributions to the structural biology of hydrogenase maturation 
      proteins.Since our first publication, where crystal structures of three Hyp 
      proteins have been determined, we have performed a series of structural studies 
      of all six Hyp proteins from a hyperthermophilic archaeon Thermococcus 
      kodakarensis, providing molecular details of each Hyp protein. We have also 
      determined the crystal structures of transient complexes between Hyp proteins 
      that are formed during the maturation process to sequentially incorporate the 
      components of the NiFe(CN)(2)CO cluster to immature large subunits of [NiFe] 
      hydrogenases. Such complexes, whose crystal structures are determined, include 
      HypA-HypB, HypA-HyhL (hydrogenase large subunit), HypC-HypD, and HypC-HypD-HypE. 
      The structures of the HypC-HypD, and HypCDE complexes reveal a sophisticated 
      process of transient formation of the HypCDE complex, providing insight into the 
      molecular basis of Fe atom cyanation. The high-resolution structures of the 
      carbamoylated and cyanated forms of HypE reveal a structural basis for the 
      biological conversion of primary amide to nitrile. The structure of the HypA-HypB 
      complex elucidates nucleotide-dependent transient complex formation between these 
      two proteins and the molecular basis of acquisition and release of labile Ni. 
      Furthermore, our recent structure analysis of a complex between HypA and immature 
      HyhL reveals that spatial rearrangement of both the N- and C-terminal tails of 
      HyhL will occur upon the [NiFe] cluster insertion, which function as a key 
      checkpoint for the maturation completion. This Account will focus on recent 
      advances in structural studies of the Hyp proteins and on mechanistic insights 
      into the [NiFe] hydrogenase maturation.
FAU - Miki, Kunio
AU  - Miki K
AUID- ORCID: 0000-0002-8381-0871
AD  - Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, 
      Kyoto 606-8502, Japan.
FAU - Atomi, Haruyuki
AU  - Atomi H
AD  - Department of Synthetic Chemistry and Biological Chemistry, Graduate School of 
      Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
FAU - Watanabe, Satoshi
AU  - Watanabe S
AUID- ORCID: 0000-0002-1130-0477
AD  - Institute of Multidisciplinary Research for Advanced Materials, Tohoku 
      University, Katahira, Sendai 980-0812, Japan.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20200331
PL  - United States
TA  - Acc Chem Res
JT  - Accounts of chemical research
JID - 0157313
RN  - EC 1.12.- (nickel-iron hydrogenase)
RN  - EC 1.12.7.2 (Hydrogenase)
SB  - IM
MH  - Biocatalysis
MH  - Hydrogenase/*chemistry/*metabolism
MH  - Protein Binding
EDAT- 2020/04/02 06:00
MHDA- 2021/04/13 06:00
CRDT- 2020/04/02 06:00
PHST- 2020/04/02 06:00 [pubmed]
PHST- 2021/04/13 06:00 [medline]
PHST- 2020/04/02 06:00 [entrez]
AID - 10.1021/acs.accounts.0c00022 [doi]
PST - ppublish
SO  - Acc Chem Res. 2020 Apr 21;53(4):875-886. doi: 10.1021/acs.accounts.0c00022. Epub 
      2020 Mar 31.