Environmental Science & Technology,
Год журнала:
2024,
Номер
unknown
Опубликована: Дек. 5, 2024
17β-estradiol
(E2)
is
one
of
the
strongest
environmental
estrogens
threatening
wildlife
and
human
health
globally.
Microbial
degradation
an
alternative
strategy
to
remediate
E2-contaminated
sites
may
be
regulated
by
ubiquitous
Fe(III)
in
eco-environments.
We
have
previously
obtained
a
high-efficiency
E2
degrader,
Novosphingobium
sp.
ES2–1,
investigated
its
metabolic
pathway
connection
with
monooxygenase
EstO1-induced
ring-B
opening;
however,
molecular
mechanisms
ring-A
cleavage
are
sorely
lacking,
especially
under
Fe(III)-aided
regulation.
Here,
extradiol
dioxygenase
EstN1
from
strain
ES2–1
involved
was
reported.
It
catalyzed
4,5-seco
reaction
4-hydroxyestrone
(4-OH-E1,
key
E2-oxidized
intermediate)
support
electron
transport
chain
consisting
ferredoxin
EstN2
reductase
EstN3,
resulting
meta-cleaved
product.
Interestingly,
Fe(III)-assisted
consolidated
opening
rings
A
B
reinforcing
expression
estO1
estN1
genes,
consequently
enhancing
metabolism.
Compared
starvation,
biodegradation
half-life
sharply
reduced
1.35
0.59
d
after
supplementation.
Simultaneously,
transcription
genes
increased
clearly
4.3
47.5
times
6.6
246.8
induction,
respectively,
accompanied
remarkable
improvement
abundance
ring-A/B
products
their
pyridine
derivatives.
These
findings
highlight
significance
regulating
microbial
remediation
at
level.
ABSTRACT
Progesterone
(PROG)
is
one
of
the
most
ubiquitous
sexual
hormones
found
as
a
pollutant
in
soil
and
water
systems.
Despite
fact
that
PROG
can
be
degraded
by
various
bacterial
species,
pathways
leading
to
its
complete
oxic
mineralization
remain
unknown.
In
this
study,
we
investigated
progesterone
catabolism
using
steroid-degrading
bacterium
Caenibius
tardaugens
model,
which
demonstrated
capacity
degrade
progestogens.
The
transcriptomic
analyses
presence
showed
overexpression
EGO55_13845
EGO55_13860
genes,
coding
Baeyer-Villiger
monooxygenase
(BVMO)
luciferase-like
(LLM),
respectively.
Both
genes
are
located
next
two
regulatory
proteins
forming
small
gene
cluster
(named
pdc
)
other
bacteria.
Mutagenic
complementation
allowed
ascertaining
involved
degradation.
To
assess
their
enzymatic
activities,
both
were
overexpressed
Escherichia
coli,
showing
they
catalyze
monooxygenation
PROG,
resulting
production
testosterone
acetate.
They
also
active
on
1,2-dehydroprogesterone,
an
intermediate
degradation,
converting
it
into
boldenone
BVMO
LLM
enzymes
functionally
redundant,
each
replace
metabolizing
PROG.
redundant
C.
explained
distinct
substrate
preferences.
Our
results
settle
for
first
time
genetic
biochemical
basis
explaining
how
recognized
channeled
9,10-seco
degradation
pathway
PROG-degrading
bacterium.
IMPORTANCE
This
study
investigates
key
steps
revealing
new
insights
process.
main
stages
examined
.
conducted
analysis
allows
identifying
pdc,
present
related
We
encoded
within
monooxygenation,
producing
activity
redundancy
difference
specificity
enzyme.
