Figure 1.
Figure 1. A: Cartoon representation of the overall fold of
Hyr1, colored and labeled according to the secondary structures.
Cys36 thiol was highlighted as sticks and the interrupted points
were colored with purple and connected with a gray dashed line.
B, C: Superposition of Hyr1 (red) upon rPtGpx5 (cyan) and
oPtGpx5 (gray), respectively. The helix 2
of rPtGpx5 and peroxidatic and resolving cysteine of all
structures were labeled. D: Hyr1 peroxidase activity assays.
Assays were performed separately for three times in the presence
of Trx2, Trr1, NADPH, and H[2]O[2], with Hyr1 (filled squares),
with Hyr1-Cys82Ser mutant (open triangles), without Hyr1 as a
null control (filled circles). Data are expressed as the
decrement of OD[340 nm] against time in minute. The error bars
represent the standard deviations.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
1058-1062)
copyright 2008.
2
of rPtGpx5 and peroxidatic and resolving cysteine of all
structures were labeled. D: Hyr1 peroxidase activity assays.
Assays were performed separately for three times in the presence
of Trx2, Trr1, NADPH, and H[2]O[2], with Hyr1 (filled squares),
with Hyr1-Cys82Ser mutant (open triangles), without Hyr1 as a
null control (filled circles). Data are expressed as the
decrement of OD[340 nm] against time in minute. The error bars
represent the standard deviations.