D00248
type: Enzyme
rlcp: p980
cath: Rossmann fold
cath: L-2-haloacid Dehalogenase; domain 2
ec: https://purl.uniprot.org/enzyme/3.8.1.2
csa: 1qh9
csa: 1qq5
macie: M0036
uniprot: Q53464
uniprot: Q60099
kegg enzyme: (S)-2-haloacid dehalogenase
kegg enzyme: 2-haloacid dehalogenase[ambiguous]
kegg enzyme: 2-haloacid halidohydrolase [ambiguous][ambiguous]
kegg enzyme: 2-haloalkanoic acid dehalogenase
kegg enzyme: 2-haloalkanoid acid halidohydrolase
kegg enzyme: 2-halocarboxylic acid dehalogenase II
kegg enzyme: DL-2-haloacid dehalogenase[ambiguous]
kegg enzyme: L-2-haloacid dehalogenase
kegg enzyme: L-DEX
kegg pathway: gamma-Hexachlorocyclohexane degradation
kegg pathway: 1,2-Dichloroethane degradation
kegg substrate: (S)-2-Haloacid
kegg substrate: H2O
kegg product: (R)-2-Hydroxyacid
kegg product: Halide
pdb: 1aq6A01
pdb: 1aq6B01
pdb: 1judA01
pdb: 1qh9A01
pdb: 1qq5A01
pdb: 1qq5B01
pdb: 1qq6A01
pdb: 1qq6B01
pdb: 1qq7A01
pdb: 1qq7B01
pdb: 1zrmA01
pdb: 1zrnA01
pdb: 1aq6A02
pdb: 1aq6B02
pdb: 1judA02
pdb: 1qh9A02
pdb: 1qq5A02
pdb: 1qq5B02
pdb: 1qq6A02
pdb: 1qq6B02
pdb: 1qq7A02
pdb: 1qq7B02
pdb: 1zrmA02
pdb: 1zrnA02
pdb bound state: Analogue
  compound: (S)-2-Haloacid
  pdb: 1aq6A01
  ligand het code: FMT_2
pdb bound state: Analogue
  compound: (S)-2-Haloacid
  pdb: 1aq6B01
  ligand het code: FMT_1
pdb bound state: Unbound
  compound: (S)-2-Haloacid
  pdb: 1judA01
pdb bound state: Unbound
  compound: (S)-2-Haloacid
  pdb: 1qh9A01
active site residues resources: Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.
active site residues resources: Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase.
active site residues resources: MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases.
active site residues resources: Q53464
active site residues resources: Q60099
references: Site-directed mutagenesis of the 2-haloalkanoic acid dehalogenase I gene from Pseudomonas sp. strain CBS3 and its effect on catalytic activity.
references: Reconsideration of the essential role of a histidine residue of L-2-halo acid dehalogenase.
references: Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues.
references: Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10.
references: Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation.
references: Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
references: Crystallization and preliminary x-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL.
references: Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate.
references: X-ray structure of a reaction intermediate of L-2-haloacid dehalogenase with L-2-chloropropionamide.
references: Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.
references: Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.
references: Dehalogenases applied to industrial-scale biocatalysis.
references: Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase.
references: Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase.
references: Identification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4.
references: Novel catalytic mechanism of nucleophilic substitution by asparagine residue involving cyanoalanine intermediate revealed by mass spectrometric monitoring of an enzyme reaction.
references: MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases.
references: Microbial dehalogenation.
references: X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily.
references: Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.
references: The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
comment: According to the literature [8], [10] & [13], the catalytic reaction proceeds as follows: (1) Asp8 (of 1aq6) acts as a nucleophile, which makes a nucleophilic attack on the carbon, which is covalently bonded to halide atom, whereas Arg39 stabilizes and accepts the leaving halide atom. (The reaction proceeds via SN2 mechanism.) (2) The intermediate is stabilized by an oxyanion hole, composed of Thr12/Ser173/Asn173 in the case of R=CH3 or larger alkyl group for the substrate, or Lys147 in the case of R=H for the substrate (see [10]). (substrate; R-CX-COOH) (3) Lys147 and Tyr153 probably modulate the activity of Asp176, by lowering its pKa. (4) Asp176 acts as a base, to activate a water. (The activated water might be stabilized by Asn173 (see [10] & [16].) (5) The activated water makes a nucleophilic attack on the carbonyl carbon of Asp8-ligand intermediate, to complete the hydrolytic reaction.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1000
catalytic domain: index.html

L-2-haloacid Dehalogenase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.164.10
catalytic domain: index.html

gamma-Hexachlorocyclohexane degradation
type: KeggPathway
references: KEGG:MAP00361

1,2-Dichloroethane degradation
type: KeggPathway
references: KEGG:MAP00631

(S)-2-Haloacid
type: KeggSubstrate
references: KEGG:C02103
compound type: carboxyl group
compound type: halide

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

(R)-2-Hydroxyacid
type: KeggProduct
references: KEGG:C02489
compound type: carbohydrate
compound type: carboxyl group

Halide
type: KeggProduct
references: KEGG:C00462
compound type: halide

1aq6A01
type: Pdb
references: 1aq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq6
catalytic residue: ASP 8;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176

1aq6B01
type: Pdb
references: 1aq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq6
catalytic residue: ASP 8;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176

1judA01
type: Pdb
references: 1jud
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jud
catalytic residue: ASP 10;THR 14;LYS 151;TYR 157;SER 175;ASN 177;ASP 180

1qh9A01
type: Pdb
references: 1qh9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh9
catalytic residue: ASP 10;THR 14;LYS 151;TYR 157;SER 175;ASN 177;ASP 180

1qq5A01
type: Pdb
references: 1qq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq5
catalytic residue: ASP 8;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176

1qq5B01
type: Pdb
references: 1qq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq5
catalytic residue: ASP 8;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176

1qq6A01
type: Pdb
references: 1qq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq6
catalytic residue: ;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176
modified residue: ASB 8(aspartic acid-4-carboxymethyl ester)

1qq6B01
type: Pdb
references: 1qq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq6
catalytic residue: ;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176
modified residue: ASB 8(aspartic acid-4-carboxymethyl ester)

1qq7A01
type: Pdb
references: 1qq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq7
catalytic residue: ;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176
modified residue: ASB 8(aspartic acid-4-carboxymethyl ester)

1qq7B01
type: Pdb
references: 1qq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq7
catalytic residue: ;THR 12;LYS 147;TYR 153;SER 171;ASN 173;ASP 176
modified residue: ASB 8(aspartic acid-4-carboxymethyl ester)

1zrmA01
type: Pdb
references: 1zrm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zrm
catalytic residue: ASP 10;THR 14;LYS 151;TYR 157; ;ASN 177;ASP 180
comment: mutant S175A

1zrnA01
type: Pdb
references: 1zrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zrn
catalytic residue: ASP 10;THR 14;LYS 151;TYR 157; ;ASN 177;ASP 180
comment: mutant S175A

1aq6A02
type: Pdb
references: 1aq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq6
catalytic residue: ARG 39

1aq6B02
type: Pdb
references: 1aq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aq6
catalytic residue: ARG 39

1judA02
type: Pdb
references: 1jud
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jud
catalytic residue: ARG 41

1qh9A02
type: Pdb
references: 1qh9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qh9
catalytic residue: ARG 41

1qq5A02
type: Pdb
references: 1qq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq5
catalytic residue: ARG 39

1qq5B02
type: Pdb
references: 1qq5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq5
catalytic residue: ARG 39

1qq6A02
type: Pdb
references: 1qq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq6
catalytic residue: ARG 39

1qq6B02
type: Pdb
references: 1qq6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq6
catalytic residue: ARG 39

1qq7A02
type: Pdb
references: 1qq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq7
catalytic residue: ARG 39

1qq7B02
type: Pdb
references: 1qq7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qq7
catalytic residue: ARG 39

1zrmA02
type: Pdb
references: 1zrm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zrm
catalytic residue: ARG 41

1zrnA02
type: Pdb
references: 1zrn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zrn
catalytic residue: ARG 41

Site-directed mutagenesis of the 2-haloalkanoic acid dehalogenase I gene from Pseudomonas sp. strain CBS3 and its effect on catalytic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8216900
journal: Biol Chem Hoppe Seyler
volume: 374
pages: 489-96
published year: 1993
authors:
  item: Schneider B
  item: Muller R
  item: Frank R
  item: Lingens F

Reconsideration of the essential role of a histidine residue of L-2-halo acid dehalogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7822238
journal: J Biochem (Tokyo)
volume: 116
pages: 248-9
published year: 1994
authors:
  item: Liu JQ
  item: Kurihara T
  item: Esaki N
  item: Soda K

Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues.
type: BibliographicResource
comment: MUTAGENESIS.
medline id: 96105006
references: http://www.ncbi.nlm.nih.gov/pubmed/7490277
journal: J Biochem (Tokyo)
volume: 117
pages: 1317-22
published year: 1995
authors:
  item: Kurihara T
  item: Liu JQ
  item: Nardi-Dei V
  item: Koshikawa H
  item: Esaki N
  item: Soda K
references: Q53464

Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8580854
journal: Protein Sci
volume: 4
pages: 2619-20
published year: 1995
authors:
  item: Ridder IS
  item: Rozeboom HJ
  item: Kingma J
  item: Janssen DB
  item: Dijkstra BW

Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8607850
journal: Biochem Biophys Res Commun
volume: 220
pages: 828-33
published year: 1996
authors:
  item: Diez A
  item: Prieto MI
  item: Alvarez MJ
  item: Bautista JM
  item: Garrido J
  item: Puyet A

Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 96355356
references: http://www.ncbi.nlm.nih.gov/pubmed/8702766
journal: J Biol Chem
volume: 271
pages: 20322-30
published year: 1996
authors:
  item: Hisano T
  item: Hata Y
  item: Fujii T
  item: Liu JQ
  item: Kurihara T
  item: Esaki N
  item: Soda K
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q53464

Crystallization and preliminary x-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8860001
journal: Proteins
volume: 24
pages: 520-2
published year: 1996
authors:
  item: Hisano T
  item: Hata Y
  item: Fujii T
  item: Liu JQ
  item: Kurihara T
  item: Esaki N
  item: Soda K

Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) AND REVISION TO 84
medline id: 98070500
references: http://www.ncbi.nlm.nih.gov/pubmed/9407083
journal: J Biol Chem
volume: 272
pages: 33015-22
published year: 1997
authors:
  item: Ridder IS
  item: Rozeboom HJ
  item: Kalk KH
  item: Janssen DB
  item: Dijkstra BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q60099

X-ray structure of a reaction intermediate of L-2-haloacid dehalogenase with L-2-chloropropionamide.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9644239
journal: J Biochem (Tokyo)
volume: 124
pages: 20-2
published year: 1998
authors:
  item: Li YF
  item: Hata Y
  item: Fujii T
  item: Kurihara T
  item: Esaki N

Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 98279020
references: http://www.ncbi.nlm.nih.gov/pubmed/9614112
journal: J Biol Chem
volume: 273
pages: 15035-44
published year: 1998
authors:
  item: Li YF
  item: Hata Y
  item: Fujii T
  item: Hisano T
  item: Nishihara M
  item: Kurihara T
  item: Esaki N
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q53464

Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10191250
journal: Biochem J
volume: 339
pages: 223-6
published year: 1999
authors:
  item: Ridder IS
  item: Dijkstra BW

Dehalogenases applied to industrial-scale biocatalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10449315
journal: Curr Opin Biotechnol
volume: 10
pages: 365-9
published year: 1999
authors:
  item: Swanson PE

Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10521454
journal: J Biol Chem
volume: 274
pages: 30672-8
published year: 1999
authors:
  item: Ridder IS
  item: Rozeboom HJ
  item: Kalk KH
  item: Dijkstra BW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10485878
journal: Proc Natl Acad Sci U S A
volume: 96
pages: 10637-42
published year: 1999
authors:
  item: Argiriadi MA
  item: Morisseau C
  item: Hammock BD
  item: Christianson DW

Identification of the dimerization domain of dehalogenase IVa of Burkholderia cepacia MBA4.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10919767
journal: Appl Environ Microbiol
volume: 66
pages: 3180-6
published year: 2000
authors:
  item: Tsang JS
  item: Pang BC

Novel catalytic mechanism of nucleophilic substitution by asparagine residue involving cyanoalanine intermediate revealed by mass spectrometric monitoring of an enzyme reaction.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11006296
journal: J Biol Chem
volume: 275
pages: 40804-9
published year: 2000
authors:
  item: Ichiyama S
  item: Kurihara T
  item: Li YF
  item: Kogure Y
  item: Tsunasawa S
  item: Esaki N
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11601995
journal: Biochemistry
volume: 40
pages: 12704-11
published year: 2001
authors:
  item: Selengut JD

Microbial dehalogenation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11404103
journal: Curr Opin Biotechnol
volume: 12
pages: 254-8
published year: 2001
authors:
  item: Janssen DB
  item: Oppentocht JE
  item: Poelarends GJ

X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15461449
journal: Biochemistry
volume: 43
pages: 12770-9
published year: 2004
authors:
  item: Peisach E
  item: Selengut JD
  item: Dunaway-Mariano D
  item: Allen KN

Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14983068
journal: Protein Eng
volume: 16
pages: 889-95
published year: 2003
authors:
  item: Stewart AJ
  item: Schmid R
  item: Blindauer CA
  item: Paisey SJ
  item: Farquharson C

The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14687572
journal: J Mol Biol
volume: 335
pages: 761-73
published year: 2004
authors:
  item: Calderone V
  item: Forleo C
  item: Benvenuti M
  item: Cristina Thaller M
  item: Maria Rossolini G
  item: Mangani S

Analogue
compound: (S)-2-Haloacid
pdb: 1qq5A01
ligand het code: FMT

Analogue
compound: (S)-2-Haloacid
pdb: 1qq5B01
ligand het code: FMT

Analogue
compound: (S)-2-Haloacid
pdb: 1aq6A02
ligand het code: FMT

IntermediateBound
pdb: 1qq6A01
ligand het code: ASB

IntermediateBound
pdb: 1qq6B01
ligand het code: ASB

IntermediateBound
pdb: 1qq7A01
ligand het code: ASB

IntermediateBound
pdb: 1qq7B01
ligand het code: ASB

IntermediateBound
pdb: 1zrmA01
ligand het code: BUA

IntermediateBound
pdb: 1zrnA01
ligand het code: ACY

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.6, p.494

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.2, p.1321

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.20328-20329

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.33020-33021

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.21

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.8, p.15041-15043

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.5, p.30676-30677

ReferenceForCatalyticMechanism
reference index: 16
reference section: SCHEME 1