Regulating ferredoxin electron transfer using nanobody and antigen interactions
RSC Chemical Biology,
Journal Year:
2025,
Volume and Issue:
6(5), P. 746 - 753
Published: Jan. 1, 2025
Fission
and
fusion
can
be
used
to
generate
new
regulatory
functions
in
proteins.
This
approach
has
been
create
ferredoxins
(Fd)
whose
cellular
electron
transfer
is
dependent
upon
small
molecule
binding.
To
investigate
whether
Fd
fragments
monitor
macromolecular
binding
reactions,
we
investigated
the
effects
of
fusing
Mastigocladus
laminosus
single
domain
antibodies,
also
known
as
nanobodies,
their
protein
antigens.
When
arising
from
fission
were
fused
green
fluorescent
(GFP)
three
different
anti-GFP
split
proteins
identified
that
supported
Fd-mediated
Fd-NADP
reductase
(FNR)
sulfite
(SIR)
Escherichia
coli.
However,
order
nanobody
antigen
affected
transfer.
Insertion
these
nanobodies
within
had
differing
on
One
domain-insertion
variant
was
unable
support
unless
it
coexpressed
with
GFP,
while
others
absence
GFP.
These
findings
show
how
Fds
engineered
so
regulated
by
macromolecules,
they
reveal
importance
exploring
homologs
strategies
when
engineering
biomolecular
switches.
Language: Английский
Simultaneous removal of carbamazepine, nitrate, and copper in a biofilm reactor filled with FeMn-modified ceramsite
Ying Zhang,
No information about this author
Miqi Ren,
No information about this author
Junfeng Su
No information about this author
et al.
Journal of Hazardous Materials,
Journal Year:
2025,
Volume and Issue:
491, P. 137871 - 137871
Published: March 9, 2025
Language: Английский
Fimsbactin Siderophores From a South African Marine Sponge Symbiont, Marinomonas sp. PE14‐40
Nompumelelo Philile Praiseworth Ikegwuoha,
No information about this author
Thea Hanekom,
No information about this author
Elzaan Booysen
No information about this author
et al.
Microbial Biotechnology,
Journal Year:
2025,
Volume and Issue:
18(5)
Published: May 1, 2025
ABSTRACT
Low
iron
levels
in
marine
habitats
necessitate
the
production
of
structurally
diverse
siderophores
by
many
bacterial
species
for
acquisition.
Siderophores
exhibit
bioactivities
ranging
from
chelation
reduction
hemochromatosis
sufferers
to
antimicrobial
activity
either
their
own
right
or
when
coupled
known
antibiotics
targeted
delivery
molecular
imaging.
Thus,
environments
are
a
sought‐after
resource
novel
that
could
have
pharmaceutical
industrial
application.
The
fimsbactins
A‐F
(
1–6
)
mixed
catechol‐hydroxamate
only
been
reported
be
produced
Acinetobacter
with
fimsbactin
biosynthetic
gene
clusters
(BGCs)
widespread
among
within
this
genus.
Here,
we
identified
putative
BGC
an
uncharacterized
isolate,
Marinomonas
sp.
PE14‐40.
Not
was
synteny
not
conserved
comparing
pathway
PE14‐40
sp.,
but
five
core
genes
found
canonical
located
elsewhere
on
genome
and
do
form
part
cluster
PE14‐40,
four
these,
fbsBCDL,
colocalized.
Through
ESI‐MS/MS
analysis
extracts
analogues
1
6
were
identified,
as
well
two
new
analogues,
7
8
,
containing
previously
unreported
L‐lysine‐derived
hydroxamate
moiety,
N
‐acetyl‐
‐hydroxycadaverine.
Feeding
experiments
using
stable
isotope‐label
L‐lysine
provided
further
evidence
‐hydroxycadaverine
moiety
.
study
demonstrates
functional
conservation
seemingly
disparate
pathways
enzyme
promiscuity's
role
producing
compounds.
Language: Английский
Regulating ferredoxin electron transfer using nanobody and antigen interactions
bioRxiv (Cold Spring Harbor Laboratory),
Journal Year:
2024,
Volume and Issue:
unknown
Published: Oct. 24, 2024
Abstract
Fission
and
fusion
can
be
used
to
generate
new
regulatory
functions
in
proteins.
This
approach
has
been
create
ferredoxins
(Fd)
whose
cellular
electron
transfer
is
dependent
upon
small
molecule
binding.
To
investigate
whether
Fd
fragments
monitor
macromolecular
binding
reactions,
we
investigated
the
effects
of
fusing
Mastigocladus
laminosus
nanobodies
their
protein
antigens.
When
arising
from
fission
were
fused
green
fluorescent
(GFP)
three
different
anti-GFP
nanobodies,
split
proteins
identified
that
supported
Fd-mediated
Fd-NADP
reductase
(FNR)
sulfite
(SIR)
Escherichia
coli
.
However,
order
nanobody
antigen
affected
transfer.
Insertion
these
within
had
differing
on
One
domain-insertion
variant
was
unable
support
unless
it
coexpressed
with
GFP,
while
others
absence
GFP.
These
findings
show
how
Fds
engineered
so
regulated
by
macromolecules,
they
reveal
importance
exploring
homologs
strategies
when
engineering
biomolecular
switches.
Language: Английский