Iron in PDB 2frv: Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Enzymatic activity of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
All present enzymatic activity of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase:
1.18.99.1;
Protein crystallography data
The structure of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase, PDB code: 2frv
was solved by
A.Volbeda,
M.Frey,
J.C.Fontecilla-Camps,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
2.54
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
112.780,
113.160,
133.910,
90.03,
90.02,
119.99
|
R / Rfree (%)
|
22.4 /
23.9
|
Other elements in 2frv:
The structure of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase also contains other interesting chemical elements:
Iron Binding Sites:
Iron binding site 1 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 1 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe265
b:2.0
occ:1.00
|
FE1
|
S:SF4265
|
0.0
|
2.0
|
1.0
|
S3
|
S:SF4265
|
2.2
|
3.1
|
1.0
|
SG
|
S:CYS219
|
2.2
|
2.0
|
1.0
|
S4
|
S:SF4265
|
2.3
|
3.3
|
1.0
|
S2
|
S:SF4265
|
2.3
|
3.2
|
1.0
|
FE4
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE2
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE3
|
S:SF4265
|
2.7
|
3.8
|
1.0
|
CB
|
S:CYS219
|
3.2
|
2.0
|
1.0
|
S1
|
S:SF4265
|
3.9
|
3.8
|
1.0
|
CA
|
S:GLY221
|
4.5
|
2.0
|
1.0
|
CA
|
S:CYS219
|
4.5
|
2.0
|
1.0
|
N
|
S:GLY221
|
4.6
|
2.0
|
1.0
|
CG2
|
S:VAL240
|
4.6
|
2.0
|
1.0
|
ND1
|
S:HIS185
|
4.7
|
6.3
|
1.0
|
SG
|
S:CYS188
|
4.7
|
2.0
|
1.0
|
CD
|
S:PRO222
|
4.8
|
2.1
|
1.0
|
SG
|
S:CYS213
|
4.8
|
7.0
|
1.0
|
C
|
S:CYS219
|
4.8
|
2.0
|
1.0
|
N
|
S:TYR215
|
4.9
|
2.0
|
1.0
|
N
|
S:LEU214
|
4.9
|
3.3
|
1.0
|
|
Iron binding site 2 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 2 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe265
b:2.0
occ:1.00
|
FE2
|
S:SF4265
|
0.0
|
2.0
|
1.0
|
ND1
|
S:HIS185
|
2.0
|
6.3
|
1.0
|
S4
|
S:SF4265
|
2.2
|
3.3
|
1.0
|
S1
|
S:SF4265
|
2.3
|
3.8
|
1.0
|
S3
|
S:SF4265
|
2.3
|
3.1
|
1.0
|
FE3
|
S:SF4265
|
2.7
|
3.8
|
1.0
|
FE4
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE1
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
CE1
|
S:HIS185
|
2.9
|
5.9
|
1.0
|
CG
|
S:HIS185
|
3.1
|
7.7
|
1.0
|
CB
|
S:HIS185
|
3.6
|
5.7
|
1.0
|
CA
|
S:HIS185
|
3.9
|
2.9
|
1.0
|
S2
|
S:SF4265
|
3.9
|
3.2
|
1.0
|
NE2
|
S:HIS185
|
4.0
|
6.2
|
1.0
|
CD2
|
S:HIS185
|
4.1
|
5.7
|
1.0
|
CD
|
S:PRO222
|
4.4
|
2.1
|
1.0
|
CB
|
S:CYS188
|
4.4
|
2.0
|
1.0
|
CG
|
S:PRO222
|
4.4
|
2.0
|
1.0
|
O
|
S:HIS185
|
4.6
|
4.3
|
1.0
|
SG
|
S:CYS188
|
4.6
|
2.0
|
1.0
|
C
|
S:HIS185
|
4.7
|
3.7
|
1.0
|
CD2
|
S:LEU191
|
4.7
|
10.4
|
1.0
|
SG
|
S:CYS219
|
4.7
|
2.0
|
1.0
|
SG
|
S:CYS213
|
4.7
|
7.0
|
1.0
|
N
|
S:PRO222
|
4.8
|
2.7
|
1.0
|
CD1
|
S:PHE194
|
4.8
|
6.0
|
1.0
|
CA
|
S:GLY221
|
4.9
|
2.0
|
1.0
|
N
|
S:HIS185
|
5.0
|
2.9
|
1.0
|
C
|
S:GLY221
|
5.0
|
2.7
|
1.0
|
|
Iron binding site 3 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 3 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe265
b:3.8
occ:1.00
|
FE3
|
S:SF4265
|
0.0
|
3.8
|
1.0
|
S2
|
S:SF4265
|
2.3
|
3.2
|
1.0
|
S1
|
S:SF4265
|
2.3
|
3.8
|
1.0
|
S4
|
S:SF4265
|
2.4
|
3.3
|
1.0
|
SG
|
S:CYS213
|
2.4
|
7.0
|
1.0
|
FE2
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE4
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE1
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
CB
|
S:CYS213
|
3.4
|
2.0
|
1.0
|
S3
|
S:SF4265
|
3.9
|
3.1
|
1.0
|
CA
|
S:CYS213
|
3.9
|
4.0
|
1.0
|
N
|
S:LEU214
|
4.0
|
3.3
|
1.0
|
CD1
|
S:PHE194
|
4.2
|
6.0
|
1.0
|
ND1
|
S:HIS185
|
4.3
|
6.3
|
1.0
|
C
|
S:CYS213
|
4.3
|
3.9
|
1.0
|
N
|
S:TYR215
|
4.3
|
2.0
|
1.0
|
CE1
|
S:HIS185
|
4.6
|
5.9
|
1.0
|
CB
|
S:TYR215
|
4.7
|
2.0
|
1.0
|
CB
|
S:PHE194
|
4.7
|
2.9
|
1.0
|
CB
|
S:ARG190
|
4.7
|
2.0
|
1.0
|
O
|
S:ARG190
|
4.8
|
7.2
|
1.0
|
SG
|
S:CYS219
|
4.8
|
2.0
|
1.0
|
SG
|
S:CYS188
|
4.8
|
2.0
|
1.0
|
CG
|
S:PHE194
|
4.8
|
4.1
|
1.0
|
CE1
|
S:PHE194
|
4.9
|
6.1
|
1.0
|
CA
|
S:TYR215
|
4.9
|
2.0
|
1.0
|
CA
|
S:LEU214
|
5.0
|
2.0
|
1.0
|
|
Iron binding site 4 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 4 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe265
b:2.0
occ:1.00
|
FE4
|
S:SF4265
|
0.0
|
2.0
|
1.0
|
S1
|
S:SF4265
|
2.2
|
3.8
|
1.0
|
SG
|
S:CYS188
|
2.3
|
2.0
|
1.0
|
S2
|
S:SF4265
|
2.3
|
3.2
|
1.0
|
S3
|
S:SF4265
|
2.3
|
3.1
|
1.0
|
FE3
|
S:SF4265
|
2.7
|
3.8
|
1.0
|
FE1
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
FE2
|
S:SF4265
|
2.7
|
2.0
|
1.0
|
CB
|
S:CYS188
|
3.0
|
2.0
|
1.0
|
S4
|
S:SF4265
|
3.9
|
3.3
|
1.0
|
CB
|
S:ARG190
|
4.1
|
2.0
|
1.0
|
ND1
|
S:HIS185
|
4.3
|
6.3
|
1.0
|
CG1
|
S:VAL240
|
4.4
|
2.0
|
1.0
|
CA
|
S:CYS188
|
4.5
|
2.9
|
1.0
|
C
|
S:ARG190
|
4.6
|
7.2
|
1.0
|
N
|
S:ARG190
|
4.7
|
5.1
|
1.0
|
CA
|
S:ARG190
|
4.7
|
4.3
|
1.0
|
N
|
S:LEU191
|
4.7
|
9.8
|
1.0
|
SG
|
S:CYS219
|
4.7
|
2.0
|
1.0
|
CG
|
S:ARG190
|
4.9
|
2.0
|
1.0
|
CA
|
S:HIS185
|
4.9
|
2.9
|
1.0
|
C
|
S:CYS188
|
4.9
|
4.3
|
1.0
|
|
Iron binding site 5 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 5 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe266
b:2.0
occ:1.00
|
FE1
|
S:F3S266
|
0.0
|
2.0
|
1.0
|
S2
|
S:F3S266
|
2.2
|
2.0
|
1.0
|
SG
|
S:CYS249
|
2.3
|
2.8
|
1.0
|
S3
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
S1
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
FE4
|
S:F3S266
|
2.7
|
2.0
|
1.0
|
FE3
|
S:F3S266
|
2.7
|
2.0
|
1.0
|
CB
|
S:CYS249
|
3.4
|
2.0
|
1.0
|
N
|
S:CYS249
|
3.8
|
2.0
|
1.0
|
S4
|
S:F3S266
|
3.9
|
2.0
|
1.0
|
CA
|
S:CYS249
|
4.0
|
2.0
|
1.0
|
O
|
S:HOH294
|
4.0
|
2.0
|
1.0
|
O
|
L:HOH5064
|
4.2
|
7.5
|
1.0
|
C
|
S:CYS249
|
4.5
|
2.0
|
1.0
|
ND2
|
S:ASN226
|
4.5
|
2.0
|
1.0
|
SG
|
S:CYS228
|
4.7
|
2.0
|
1.0
|
N
|
S:SER250
|
4.7
|
2.0
|
1.0
|
SG
|
S:CYS246
|
4.8
|
2.0
|
1.0
|
CE
|
L:LYS216
|
5.0
|
2.0
|
1.0
|
|
Iron binding site 6 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 6 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe266
b:2.0
occ:1.00
|
FE3
|
S:F3S266
|
0.0
|
2.0
|
1.0
|
S4
|
S:F3S266
|
2.2
|
2.0
|
1.0
|
S3
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
S1
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
SG
|
S:CYS246
|
2.3
|
2.0
|
1.0
|
FE1
|
S:F3S266
|
2.7
|
2.0
|
1.0
|
FE4
|
S:F3S266
|
2.8
|
2.0
|
1.0
|
CB
|
S:CYS246
|
3.3
|
2.0
|
1.0
|
CA
|
S:CYS246
|
3.6
|
2.0
|
1.0
|
S2
|
S:F3S266
|
3.9
|
2.0
|
1.0
|
N
|
S:ILE247
|
3.9
|
2.0
|
1.0
|
C
|
S:CYS246
|
4.1
|
2.0
|
1.0
|
N
|
S:ALA248
|
4.2
|
2.0
|
1.0
|
N
|
S:CYS249
|
4.5
|
2.0
|
1.0
|
CG2
|
S:THR224
|
4.6
|
2.0
|
1.0
|
SG
|
S:CYS228
|
4.7
|
2.0
|
1.0
|
NE2
|
L:GLN221
|
4.8
|
2.0
|
1.0
|
CA
|
S:ALA248
|
4.8
|
2.0
|
1.0
|
SG
|
S:CYS249
|
4.8
|
2.8
|
1.0
|
CG2
|
S:VAL184
|
4.9
|
2.0
|
1.0
|
C
|
S:ILE247
|
4.9
|
2.0
|
1.0
|
CA
|
S:ILE247
|
4.9
|
2.0
|
1.0
|
N
|
S:CYS246
|
5.0
|
2.2
|
1.0
|
CG
|
S:PRO239
|
5.0
|
2.0
|
1.0
|
|
Iron binding site 7 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 7 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe266
b:2.0
occ:1.00
|
FE4
|
S:F3S266
|
0.0
|
2.0
|
1.0
|
S2
|
S:F3S266
|
2.2
|
2.0
|
1.0
|
SG
|
S:CYS228
|
2.2
|
2.0
|
1.0
|
S3
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
S4
|
S:F3S266
|
2.3
|
2.0
|
1.0
|
FE1
|
S:F3S266
|
2.7
|
2.0
|
1.0
|
FE3
|
S:F3S266
|
2.8
|
2.0
|
1.0
|
CB
|
S:CYS228
|
3.4
|
2.0
|
1.0
|
S1
|
S:F3S266
|
3.9
|
2.0
|
1.0
|
ND2
|
S:ASN226
|
4.1
|
2.0
|
1.0
|
CE2
|
S:PHE233
|
4.3
|
2.0
|
1.0
|
O
|
S:HOH294
|
4.4
|
2.0
|
1.0
|
CZ
|
S:PHE233
|
4.5
|
2.0
|
1.0
|
CG2
|
S:VAL184
|
4.6
|
2.0
|
1.0
|
CG
|
S:ASN226
|
4.6
|
2.0
|
1.0
|
SG
|
S:CYS249
|
4.7
|
2.8
|
1.0
|
CB
|
S:ASN226
|
4.8
|
2.0
|
1.0
|
CA
|
S:CYS228
|
4.8
|
2.0
|
1.0
|
CG
|
S:PRO239
|
4.8
|
2.0
|
1.0
|
CD
|
S:PRO239
|
4.8
|
2.4
|
1.0
|
SG
|
S:CYS246
|
4.8
|
2.0
|
1.0
|
|
Iron binding site 8 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 8 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe267
b:2.0
occ:1.00
|
FE1
|
S:SF4267
|
0.0
|
2.0
|
1.0
|
S2
|
S:SF4267
|
2.2
|
2.0
|
1.0
|
SG
|
S:CYS17
|
2.2
|
2.0
|
1.0
|
S4
|
S:SF4267
|
2.2
|
2.0
|
1.0
|
S3
|
S:SF4267
|
2.4
|
2.0
|
1.0
|
FE3
|
S:SF4267
|
2.6
|
2.8
|
1.0
|
FE2
|
S:SF4267
|
2.7
|
2.0
|
1.0
|
FE4
|
S:SF4267
|
2.7
|
2.0
|
1.0
|
CB
|
S:CYS17
|
3.3
|
2.0
|
1.0
|
S1
|
S:SF4267
|
3.9
|
2.0
|
1.0
|
N
|
S:CYS17
|
3.9
|
2.0
|
1.0
|
NE2
|
L:HIS219
|
4.0
|
2.0
|
1.0
|
CA
|
S:CYS17
|
4.1
|
2.0
|
1.0
|
N
|
S:GLY19
|
4.1
|
2.0
|
1.0
|
CA
|
S:GLY19
|
4.5
|
2.0
|
1.0
|
N
|
S:THR18
|
4.5
|
2.9
|
1.0
|
C
|
S:CYS17
|
4.5
|
2.0
|
1.0
|
N
|
S:CYS20
|
4.7
|
2.0
|
1.0
|
O
|
S:HOH330
|
4.7
|
5.3
|
1.0
|
SG
|
S:CYS112
|
4.7
|
2.0
|
1.0
|
CD2
|
L:HIS219
|
4.7
|
2.0
|
1.0
|
SG
|
S:CYS148
|
4.8
|
2.0
|
1.0
|
C
|
S:GLY19
|
4.9
|
2.0
|
1.0
|
CG
|
L:ARG63
|
4.9
|
2.0
|
1.0
|
SG
|
S:CYS20
|
4.9
|
2.0
|
1.0
|
|
Iron binding site 9 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 9 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe267
b:2.0
occ:1.00
|
FE2
|
S:SF4267
|
0.0
|
2.0
|
1.0
|
SG
|
S:CYS112
|
2.2
|
2.0
|
1.0
|
S3
|
S:SF4267
|
2.3
|
2.0
|
1.0
|
S1
|
S:SF4267
|
2.3
|
2.0
|
1.0
|
S4
|
S:SF4267
|
2.3
|
2.0
|
1.0
|
FE3
|
S:SF4267
|
2.7
|
2.8
|
1.0
|
FE4
|
S:SF4267
|
2.7
|
2.0
|
1.0
|
FE1
|
S:SF4267
|
2.7
|
2.0
|
1.0
|
CB
|
S:CYS112
|
3.2
|
2.0
|
1.0
|
S2
|
S:SF4267
|
3.9
|
2.0
|
1.0
|
O
|
S:HOH298
|
4.1
|
2.0
|
1.0
|
N
|
S:CYS112
|
4.1
|
2.0
|
1.0
|
O
|
S:HOH305
|
4.2
|
2.0
|
1.0
|
O
|
S:HOH330
|
4.2
|
5.3
|
1.0
|
CA
|
S:CYS112
|
4.3
|
2.0
|
1.0
|
SG
|
S:CYS148
|
4.6
|
2.0
|
1.0
|
SG
|
S:CYS20
|
4.7
|
2.0
|
1.0
|
SG
|
S:CYS17
|
4.8
|
2.0
|
1.0
|
N
|
S:CYS17
|
4.9
|
2.0
|
1.0
|
|
Iron binding site 10 out
of 72 in 2frv
Go back to
Iron Binding Sites List in 2frv
Iron binding site 10 out
of 72 in the Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Crystal Structure of the Oxidized Form of Ni-Fe Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Fe267
b:2.8
occ:1.00
|
FE3
|
S:SF4267
|
0.0
|
2.8
|
1.0
|
S4
|
S:SF4267
|
2.2
|
2.0
|
1.0
|
S2
|
S:SF4267
|
2.3
|
2.0
|
1.0
|
S1
|
S:SF4267
|
2.3
|
2.0
|
1.0
|
SG
|
S:CYS148
|
2.4
|
2.0
|
1.0
|
FE1
|
S:SF4267
|
2.6
|
2.0
|
1.0
|
FE2
|
S:SF4267
|
2.7
|
2.0
|
1.0
|
FE4
|
S:SF4267
|
2.8
|
2.0
|
1.0
|
CB
|
S:CYS148
|
3.5
|
2.0
|
1.0
|
CA
|
S:CYS148
|
3.5
|
2.0
|
1.0
|
S3
|
S:SF4267
|
3.9
|
2.0
|
1.0
|
C
|
S:CYS148
|
3.9
|
3.1
|
1.0
|
O
|
S:HOH305
|
3.9
|
2.0
|
1.0
|
O
|
S:CYS148
|
4.2
|
3.0
|
1.0
|
SG
|
S:CYS112
|
4.4
|
2.0
|
1.0
|
CG
|
L:ARG63
|
4.4
|
2.0
|
1.0
|
N
|
S:PRO149
|
4.4
|
3.4
|
1.0
|
NE2
|
L:HIS219
|
4.5
|
2.0
|
1.0
|
CD2
|
L:HIS219
|
4.5
|
2.0
|
1.0
|
SG
|
S:CYS17
|
4.6
|
2.0
|
1.0
|
NE
|
L:ARG63
|
4.7
|
2.0
|
1.0
|
O
|
S:GLY147
|
4.8
|
2.0
|
1.0
|
CA
|
S:PRO149
|
4.8
|
2.5
|
1.0
|
SG
|
S:CYS20
|
4.8
|
2.0
|
1.0
|
N
|
S:CYS148
|
4.9
|
2.6
|
1.0
|
|
Reference:
A.Volbeda,
E.Garcin,
C.Piras,
A.L.De Lacey,
V.M.Fernandez,
E.C.Hatchikian,
M.Frey,
J.C.Fontecilla-Camps.
Structure of the [Nife] Hydrogenase Active Site: Evidence For Biologically Uncommon Fe Ligands J.Am.Chem.Soc. V. 118 12989 1996.
ISSN: ISSN 0002-7863
Page generated: Sat Aug 3 21:42:01 2024
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