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Iron in PDB 29xz: Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site

Enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site

All present enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site:
7.1.1.8;

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site (pdb code 29xz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 10 binding sites of Iron where determined in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site, PDB code: 29xz:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 10 in 29xz

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Iron binding site 1 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:108.0
occ:1.00
 FE1 A:FES501 0.0 108.0 1.0
S1 A:FES501 2.2 103.5 1.0
S2 A:FES501 2.2 102.6 1.0
SG A:CYS133 2.3 96.2 1.0
SG A:CYS153 2.3 97.7 1.0
FE2 A:FES501 2.7 109.9 1.0
CB A:CYS133 3.2 85.2 1.0
CB A:CYS153 3.3 90.0 1.0
CB A:HIS135 3.9 91.6 1.0
CB A:CYS138 4.0 98.6 1.0
ND1 A:HIS135 4.3 94.6 1.0
CB A:CYS155 4.5 101.3 1.0
OG A:SER158 4.5 96.3 1.0
CG A:HIS135 4.6 91.1 1.0
N A:CYS138 4.6 93.9 1.0
N A:LEU136 4.6 92.5 1.0
CA A:CYS133 4.6 81.8 1.0
CB A:SER158 4.7 95.6 1.0
ND1 A:HIS156 4.7 98.7 1.0
CA A:CYS153 4.7 93.3 1.0
CA A:CYS138 4.8 90.2 1.0
N A:HIS135 4.9 91.3 1.0
O A:CYS138 4.9 90.3 1.0
SG A:CYS138 4.9 135.1 1.0
N A:HIS156 4.9 99.2 1.0
CA A:HIS135 4.9 89.8 1.0

Iron binding site 2 out of 10 in 29xz

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Iron binding site 2 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:109.9
occ:1.00
 FE2 A:FES501 0.0 109.9 1.0
ND1 A:HIS135 2.2 94.6 1.0
ND1 A:HIS156 2.2 98.7 1.0
S2 A:FES501 2.2 102.6 1.0
S1 A:FES501 2.2 103.5 1.0
FE1 A:FES501 2.7 108.0 1.0
CE1 A:HIS135 3.1 90.2 1.0
CG A:HIS156 3.1 98.4 1.0
CG A:HIS135 3.2 91.1 1.0
CE1 A:HIS156 3.2 99.1 1.0
CB A:HIS156 3.3 96.9 1.0
CB A:HIS135 3.5 91.6 1.0
N A:HIS156 3.8 99.2 1.0
CB A:CYS155 4.0 101.3 1.0
CA A:HIS156 4.2 97.2 1.0
NE2 A:HIS135 4.2 87.6 1.0
CD2 A:HIS156 4.3 96.5 1.0
NE2 A:HIS156 4.3 97.4 1.0
CD2 A:HIS135 4.3 89.8 1.0
N A:LEU136 4.4 92.5 1.0
SG A:CYS153 4.4 97.7 1.0
C A:CYS155 4.4 100.8 1.0
SG A:CYS133 4.5 96.2 1.0
CB A:LEU136 4.6 91.4 1.0
CA A:HIS135 4.8 89.8 1.0
CA A:CYS155 4.8 100.2 1.0
OG A:SER158 4.8 96.3 1.0
C A:HIS135 4.9 92.9 1.0
CG A:LEU136 4.9 94.0 1.0
CG A:PRO170 5.0 90.5 1.0
C A:HIS156 5.0 100.0 1.0

Iron binding site 3 out of 10 in 29xz

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Iron binding site 3 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:77.5
occ:1.00
 FE B:HEM501 0.0 77.5 1.0
NC B:HEM501 2.0 57.4 1.0
ND B:HEM501 2.0 57.6 1.0
NB B:HEM501 2.0 55.3 1.0
NA B:HEM501 2.0 56.7 1.0
NE2 B:HIS198 2.2 53.9 1.0
NE2 B:HIS97 2.2 55.5 1.0
C4B B:HEM501 3.1 51.7 1.0
C1C B:HEM501 3.1 53.3 1.0
C4D B:HEM501 3.1 55.7 1.0
C4C B:HEM501 3.1 55.4 1.0
C1A B:HEM501 3.1 51.4 1.0
C1B B:HEM501 3.1 52.1 1.0
C1D B:HEM501 3.1 57.5 1.0
C4A B:HEM501 3.1 52.0 1.0
CE1 B:HIS198 3.1 51.1 1.0
CE1 B:HIS97 3.1 53.5 1.0
CD2 B:HIS97 3.2 52.3 1.0
CD2 B:HIS198 3.3 52.7 1.0
CHC B:HEM501 3.4 50.6 1.0
CHA B:HEM501 3.4 52.2 1.0
CHD B:HEM501 3.4 56.3 1.0
CHB B:HEM501 3.4 49.5 1.0
ND1 B:HIS198 4.2 57.0 1.0
ND1 B:HIS97 4.3 57.4 1.0
C3B B:HEM501 4.3 54.2 1.0
C3D B:HEM501 4.3 58.7 1.0
C2B B:HEM501 4.3 55.3 1.0
C2D B:HEM501 4.3 56.7 1.0
C2A B:HEM501 4.3 54.3 1.0
C2C B:HEM501 4.3 53.3 1.0
C3A B:HEM501 4.3 53.4 1.0
C3C B:HEM501 4.3 53.1 1.0
CG B:HIS97 4.4 57.2 1.0
CG B:HIS198 4.4 57.2 1.0

Iron binding site 4 out of 10 in 29xz

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Iron binding site 4 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:78.7
occ:1.00
 FE B:HEM502 0.0 78.7 1.0
ND B:HEM502 2.0 63.7 1.0
NA B:HEM502 2.0 62.5 1.0
NC B:HEM502 2.0 60.1 1.0
NB B:HEM502 2.0 62.8 1.0
NE2 B:HIS212 2.3 59.4 1.0
NE2 B:HIS111 2.3 61.1 1.0
C4C B:HEM502 3.0 56.3 1.0
C1D B:HEM502 3.1 59.3 1.0
C4A B:HEM502 3.1 62.3 1.0
C1C B:HEM502 3.1 59.1 1.0
C4D B:HEM502 3.1 60.7 1.0
C1A B:HEM502 3.1 57.7 1.0
C1B B:HEM502 3.1 56.8 1.0
C4B B:HEM502 3.1 58.7 1.0
CD2 B:HIS212 3.1 56.7 1.0
CD2 B:HIS111 3.1 60.9 1.0
CE1 B:HIS212 3.3 60.7 1.0
CE1 B:HIS111 3.4 60.5 1.0
CHD B:HEM502 3.4 57.0 1.0
CHB B:HEM502 3.4 57.5 1.0
CHA B:HEM502 3.4 57.7 1.0
CHC B:HEM502 3.4 55.6 1.0
C3C B:HEM502 4.3 59.3 1.0
C2C B:HEM502 4.3 58.9 1.0
C3A B:HEM502 4.3 62.9 1.0
C2A B:HEM502 4.3 62.2 1.0
C2D B:HEM502 4.3 60.8 1.0
C3D B:HEM502 4.3 62.0 1.0
C2B B:HEM502 4.3 53.5 1.0
C3B B:HEM502 4.3 55.1 1.0
CG B:HIS212 4.3 62.0 1.0
ND1 B:HIS212 4.3 66.8 1.0
CG B:HIS111 4.3 61.2 1.0
ND1 B:HIS111 4.4 62.9 1.0

Iron binding site 5 out of 10 in 29xz

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Iron binding site 5 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:81.8
occ:1.00
 FE C:HEC501 0.0 81.8 1.0
NA C:HEC501 2.0 65.8 1.0
NC C:HEC501 2.0 70.0 1.0
NB C:HEC501 2.1 66.1 1.0
ND C:HEC501 2.1 68.7 1.0
NE2 C:HIS38 2.2 63.7 1.0
SD C:MET183 2.3 71.8 1.0
CE1 C:HIS38 2.9 60.3 1.0
C1A C:HEC501 3.0 64.7 1.0
C4C C:HEC501 3.1 66.1 1.0
C1C C:HEC501 3.1 66.7 1.0
C4D C:HEC501 3.1 66.1 1.0
C4B C:HEC501 3.1 64.5 1.0
C4A C:HEC501 3.1 62.2 1.0
C1D C:HEC501 3.1 67.7 1.0
C1B C:HEC501 3.1 61.9 1.0
CD2 C:HIS38 3.3 63.3 1.0
CE C:MET183 3.4 64.9 1.0
CHA C:HEC501 3.4 65.5 1.0
CHC C:HEC501 3.4 64.5 1.0
CHD C:HEC501 3.4 65.5 1.0
CHB C:HEC501 3.5 60.4 1.0
CG C:MET183 3.5 70.2 1.0
ND1 C:HIS38 4.1 58.8 1.0
CB C:MET183 4.3 71.8 1.0
C2A C:HEC501 4.3 65.0 1.0
C2C C:HEC501 4.3 67.2 1.0
C3C C:HEC501 4.3 68.8 1.0
C3A C:HEC501 4.3 62.1 1.0
C3B C:HEC501 4.3 62.2 1.0
C3D C:HEC501 4.3 67.7 1.0
C2B C:HEC501 4.3 60.5 1.0
C2D C:HEC501 4.3 68.9 1.0
CG C:HIS38 4.3 61.7 1.0

Iron binding site 6 out of 10 in 29xz

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Iron binding site 6 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:109.3
occ:1.00
 FE1 D:FES501 0.0 109.3 1.0
S1 D:FES501 2.2 104.3 1.0
S2 D:FES501 2.2 104.0 1.0
SG D:CYS133 2.3 97.9 1.0
SG D:CYS153 2.3 98.9 1.0
FE2 D:FES501 2.7 109.8 1.0
CB D:CYS133 3.2 85.4 1.0
CB D:CYS153 3.3 90.5 1.0
CB D:HIS135 3.9 91.7 1.0
CB D:CYS138 4.0 98.7 1.0
ND1 D:HIS135 4.3 94.4 1.0
CB D:CYS155 4.5 100.7 1.0
OG D:SER158 4.5 97.7 1.0
CG D:HIS135 4.6 91.0 1.0
N D:CYS138 4.6 94.0 1.0
N D:LEU136 4.6 92.8 1.0
CA D:CYS133 4.6 82.2 1.0
CB D:SER158 4.7 96.0 1.0
ND1 D:HIS156 4.7 98.3 1.0
CA D:CYS153 4.7 93.4 1.0
CA D:CYS138 4.8 90.0 1.0
N D:HIS135 4.9 91.5 1.0
O D:CYS138 4.9 90.8 1.0
SG D:CYS138 4.9 135.7 1.0
N D:HIS156 4.9 98.6 1.0
CA D:HIS135 4.9 90.0 1.0

Iron binding site 7 out of 10 in 29xz

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Iron binding site 7 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:109.8
occ:1.00
 FE2 D:FES501 0.0 109.8 1.0
ND1 D:HIS135 2.2 94.4 1.0
ND1 D:HIS156 2.2 98.3 1.0
S2 D:FES501 2.2 104.0 1.0
S1 D:FES501 2.2 104.3 1.0
FE1 D:FES501 2.7 109.3 1.0
CE1 D:HIS135 3.1 90.3 1.0
CG D:HIS156 3.1 97.3 1.0
CG D:HIS135 3.2 91.0 1.0
CE1 D:HIS156 3.2 98.1 1.0
CB D:HIS156 3.3 95.7 1.0
CB D:HIS135 3.5 91.7 1.0
N D:HIS156 3.8 98.6 1.0
CB D:CYS155 4.0 100.7 1.0
CA D:HIS156 4.2 96.6 1.0
NE2 D:HIS135 4.2 87.3 1.0
CD2 D:HIS156 4.3 94.4 1.0
NE2 D:HIS156 4.3 95.4 1.0
CD2 D:HIS135 4.3 89.6 1.0
N D:LEU136 4.4 92.8 1.0
SG D:CYS153 4.4 98.9 1.0
C D:CYS155 4.4 99.9 1.0
SG D:CYS133 4.5 97.9 1.0
CB D:LEU136 4.6 91.7 1.0
CA D:HIS135 4.8 90.0 1.0
CA D:CYS155 4.8 99.5 1.0
OG D:SER158 4.8 97.7 1.0
C D:HIS135 4.9 92.8 1.0
CG D:LEU136 4.9 94.2 1.0
CG D:PRO170 5.0 91.4 1.0
C D:HIS156 5.0 100.2 1.0

Iron binding site 8 out of 10 in 29xz

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Iron binding site 8 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe501

b:77.3
occ:1.00
 FE E:HEM501 0.0 77.3 1.0
NC E:HEM501 2.0 57.8 1.0
ND E:HEM501 2.0 57.2 1.0
NB E:HEM501 2.0 55.2 1.0
NA E:HEM501 2.0 57.3 1.0
NE2 E:HIS198 2.2 54.1 1.0
NE2 E:HIS97 2.2 55.3 1.0
C4B E:HEM501 3.1 51.7 1.0
C1C E:HEM501 3.1 53.3 1.0
C4D E:HEM501 3.1 56.0 1.0
C4C E:HEM501 3.1 54.8 1.0
C1A E:HEM501 3.1 51.9 1.0
C1B E:HEM501 3.1 52.4 1.0
C1D E:HEM501 3.1 57.8 1.0
C4A E:HEM501 3.1 53.0 1.0
CE1 E:HIS198 3.1 51.4 1.0
CE1 E:HIS97 3.1 53.2 1.0
CD2 E:HIS97 3.2 52.0 1.0
CD2 E:HIS198 3.3 53.0 1.0
CHC E:HEM501 3.4 50.5 1.0
CHA E:HEM501 3.4 52.3 1.0
CHD E:HEM501 3.4 56.2 1.0
CHB E:HEM501 3.4 49.6 1.0
ND1 E:HIS198 4.2 57.1 1.0
ND1 E:HIS97 4.3 57.2 1.0
C3B E:HEM501 4.3 54.2 1.0
C3D E:HEM501 4.3 59.6 1.0
C2B E:HEM501 4.3 56.2 1.0
C2D E:HEM501 4.3 57.0 1.0
C2A E:HEM501 4.3 54.7 1.0
C2C E:HEM501 4.3 53.1 1.0
C3A E:HEM501 4.3 54.0 1.0
C3C E:HEM501 4.3 52.2 1.0
CG E:HIS97 4.4 56.5 1.0
CG E:HIS198 4.4 57.7 1.0

Iron binding site 9 out of 10 in 29xz

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Iron binding site 9 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe502

b:79.8
occ:1.00
 FE E:HEM502 0.0 79.8 1.0
ND E:HEM502 2.0 64.2 1.0
NA E:HEM502 2.0 62.9 1.0
NC E:HEM502 2.0 60.7 1.0
NB E:HEM502 2.0 63.5 1.0
NE2 E:HIS212 2.3 59.8 1.0
NE2 E:HIS111 2.3 61.9 1.0
C4C E:HEM502 3.0 57.0 1.0
C1D E:HEM502 3.1 60.0 1.0
C4A E:HEM502 3.1 62.5 1.0
C4D E:HEM502 3.1 61.1 1.0
C1C E:HEM502 3.1 59.5 1.0
C1A E:HEM502 3.1 58.2 1.0
C1B E:HEM502 3.1 57.1 1.0
C4B E:HEM502 3.1 59.2 1.0
CD2 E:HIS212 3.1 57.1 1.0
CD2 E:HIS111 3.1 61.5 1.0
CE1 E:HIS212 3.3 60.8 1.0
CE1 E:HIS111 3.4 61.3 1.0
CHD E:HEM502 3.4 57.4 1.0
CHB E:HEM502 3.4 57.4 1.0
CHA E:HEM502 3.4 58.4 1.0
CHC E:HEM502 3.4 56.3 1.0
C3C E:HEM502 4.3 60.0 1.0
C2C E:HEM502 4.3 59.3 1.0
C3A E:HEM502 4.3 63.5 1.0
C2A E:HEM502 4.3 63.0 1.0
C2D E:HEM502 4.3 61.8 1.0
C3D E:HEM502 4.3 62.7 1.0
C2B E:HEM502 4.3 54.2 1.0
C3B E:HEM502 4.3 55.7 1.0
CG E:HIS212 4.3 62.6 1.0
ND1 E:HIS212 4.3 67.3 1.0
CG E:HIS111 4.3 61.6 1.0
ND1 E:HIS111 4.4 63.5 1.0

Iron binding site 10 out of 10 in 29xz

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Iron binding site 10 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.16 A Resolution with Water Molecules and Quinone in the Quinone Reduction Site within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:82.8
occ:1.00
 FE F:HEC501 0.0 82.8 1.0
NA F:HEC501 2.0 63.9 1.0
NC F:HEC501 2.0 69.3 1.0
NB F:HEC501 2.1 64.6 1.0
ND F:HEC501 2.1 67.1 1.0
NE2 F:HIS38 2.2 61.6 1.0
SD F:MET183 2.3 72.2 1.0
CE1 F:HIS38 2.9 56.9 1.0
C1A F:HEC501 3.0 62.1 1.0
C1C F:HEC501 3.1 64.9 1.0
C4C F:HEC501 3.1 63.8 1.0
C4D F:HEC501 3.1 63.5 1.0
C4B F:HEC501 3.1 62.6 1.0
C4A F:HEC501 3.1 59.2 1.0
C1D F:HEC501 3.1 65.5 1.0
C1B F:HEC501 3.1 59.4 1.0
CD2 F:HIS38 3.3 61.3 1.0
CE F:MET183 3.4 61.8 1.0
CHA F:HEC501 3.4 62.5 1.0
CHC F:HEC501 3.4 62.1 1.0
CHD F:HEC501 3.4 62.9 1.0
CHB F:HEC501 3.5 57.0 1.0
CG F:MET183 3.5 67.7 1.0
ND1 F:HIS38 4.1 55.2 1.0
CB F:MET183 4.3 69.6 1.0
C2A F:HEC501 4.3 62.8 1.0
C2C F:HEC501 4.3 65.6 1.0
C3C F:HEC501 4.3 67.4 1.0
C3A F:HEC501 4.3 59.5 1.0
C3B F:HEC501 4.3 59.4 1.0
C3D F:HEC501 4.3 64.5 1.0
C2B F:HEC501 4.3 57.8 1.0
C2D F:HEC501 4.3 66.4 1.0
CG F:HIS38 4.3 58.7 1.0

Reference:

R.Pietras, A.Wojcik-Augustyn, B.Mielecki, M.Sarewicz, M.Jaciuk, L.Koziej, S.Glatt, A.Osyczka. Distinct Ubiquinone Binding at the Oxidation and Reduction Sites of Cytochrome Bc 1. Proc.Natl.Acad.Sci.Usa V. 123 42123 2026.
ISSN: ESSN 1091-6490
PubMed: 42679026
DOI: 10.1073/PNAS.2618242123
Page generated: Sun Oct 4 09:43:37 2026

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